ENZYME:1.3.1.33 ID 1.3.1.33 DE PROTOCHLOROPHYLLIDE REDUCTASE. AN NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE. CA CHLOROPHYLLIDE A + NADP(+) = PROTOCHLOROPHYLLIDE + NADPH. CC -!- CATALYSES A LIGHT-DEPENDENT TRANS-REDUCTION OF THE D-RING OF CC PROTOCHLOROPHYLLIDE; THE PRODUCT HAS THE (7S,8S)-CONFIGURATION. DR P26163, BCHB_RHOCA; P26237, BCHL_RHOCA; P26164, BCHN_RHOCA; DR P37843, CHLB_ARAHE; P37844, CHLB_BAZTR; P37823, CHLB_CHLHU; DR P17652, CHLB_CHLMO; P37824, CHLB_CHLPT; P36437, CHLB_CHLRE; DR P48099, CHLB_CYAPA; P37846, CHLB_EPHAL; P37845, CHLB_EQUAR; DR P36208, CHLB_GINBI; P37847, CHLB_LYCAN; P37848, CHLB_LYCCO; DR P26238, CHLB_MARPO; P37849, CHLB_METGY; P37850, CHLB_NEPEX; DR P37851, CHLB_OSMCL; P37853, CHLB_PICMA; Q00864, CHLB_PINTH; DR P37854, CHLB_PLESC; P37852, CHLB_POLCU; P51278, CHLB_PORPU; DR P37855, CHLB_SALAU; P37856, CHLB_SELMO; P37857, CHLB_ZAMFI; DR P29683, CHLN_CHLRE; P48100, CHLN_CYAPA; P26156, CHLN_MARPO; DR P26180, CHLN_PINCO; P41646, CHLN_PINTH; Q04607, CHLN_PLEBO; DR P51188, CHLN_PORPU; P54208, CHLN_SYNP7; P28372, CHLN_SYNY3; DR P21218, PCR_ARATH ; P15904, PCR_AVESA ; P13653, PCR_HORVU ; DR Q01289, PCR_PEA ; PIR:S04783 >P1;S04783 protochlorophyllide reductase (EC 1.3.1.33) precursor - barley C;Species: Hordeum vulgare (barley) C;Date: 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 28-Oct-1994 C;Accession: S04783 R;Schulz, R.; Steinmueller, K.; Klaas, M.; Forreiter, C.; Rasmussen, S.; Hiller, C.; Apel, K. Mol. Gen. Genet. 217, 355-361, 1989 A;Title: Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. A;Reference number: S04783; MUID:89364719 A;Accession: S04783 A;Molecule type: mRNA A;Residues: 1-388 A;Cross-references: EMBL:X15869 A;Note: part of this sequence, including the amino end of the mature protein, was confirmed by protein sequencing C;Keywords: chloroplast; oxidoreductase F;1-74/Domain: transit peptide (chloroplast) #status predicted F;75-388/Product: protochlorophyllide reductase #status experimental >S04783 MALQLLPSTLSVPKKGSSMGAVAVKDTAAFLGVSSKAKKASLAVRTQVATAPSPVTTSPG STASSPSGKKTLRQGVVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAG MADGSYTVMHLDLASLDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARTPTFTADGHEMS VGVNHLGHFLLARLLMEDLQKSDYPSRRMVIVGSITGNSNTLAGNVPPKASLGDLRGLAG GLSGASGSAMIDGDESFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFSSLYPGCIATT GLFREHIPLFRTLFPPFQKFVTKGFVSEAESGKRLAQVVAEPVLTKSGVYWSWNKDSASF ENQLSQEASDPEKARKVWELSEKLVGLA PIR:S08406 >F1;S08406 protochlorophyllide reductase (EC 1.3.1.33) - oat (fragment) C;Species: Avena sativa (oat) C;Date: 29-Jan-1993 #sequence_revision 29-Jan-1993 #text_change 28-Apr-1993 C;Accession: S08406; S27099 R;Darrah, P.M.; Kay, S.A.; Teakle, G.R.; Griffiths, W.T. Biochem. J. 265, 789-798, 1990 A;Title: Cloning and sequencing of protochlorophyllide reductase. A;Reference number: S08406; MUID:90165879 A;Accession: S08406 A;Molecule type: mRNA A;Residues: 1-313 A;Cross-references: EMBL:X17067 A;Accession: S27099 A;Molecule type: protein A;Residues: 175,'X',177-181 C;Keywords: chloroplast; NADP; oxidoreductase >S08406 VVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAGMADGSYTVMHLDLAS LDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARKPTFTAEGVEMSVGVNHLGHFLLARLL LEDLQKSDYPSRRLVIVGSITGNDNTLAGNVPPKANLGDLRGLAGGLTGASGSAMIDGDE SFDGAKAYKDSKVCNMLTMQEFHRRYHEDTGITFSSLYPGCIATTGLFREHIPLFRTLFP PFQKFVTKGFVSEAESGKRLAQVVGEPSLTKSGVYWSWNKDSASFENQLSQEASDPEKAR KVWELSEKLVGLA PIR:S20941 >P1;S20941 protochlorophyllide reductase (EC 1.3.1.33) precursor - garden pea C;Species: Pisum sativum (garden pea) C;Date: 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 01-Nov-1996 C;Accession: S20941; S71412 R;Spano, A.J.; He, Z.; Michel, H.; Hunt, D.F.; Timko, M.P. Plant Mol. Biol. 18, 967-972, 1992 A;Title: Molecular cloning, nuclear gene structure, and developmental expression of NADPH: protochlorophyllide oxidoreductase in pea (Pisum sativum L.). A;Reference number: S20941; MUID:92256817 A;Accession: S20941 A;Molecule type: DNA A;Residues: 1-400 A;Cross-references: EMBL:X63060 A;Accession: S71412 A;Molecule type: protein A;Residues: 65-76 C;Genetics: A;Gene: lpcr A;Genome: nuclear A;Introns: 18/3; 52/3; 230/1; 349/3 C;Keywords: chloroplast; NADP; oxidoreductase F;1-64/Domain: transit peptide (chloroplast) #status experimental F;65-400/Product: protochlorophyllide reductase #status experimental >S20941 MALQTASMLPASFSIPKEGKIGASLKDSTLFGVSSLSDSLKGDFTSSALRCKRELRQKVG AVRAETAAPATPAVNKSSSEGKKTLRKGNVVITGASSGLGLATAKALAESGKWHVIMACR DYLKAARAAKSAGLAKENYTIMHLDLASLDSVRQFVDNFRRSEMPLDVLINNAAVYFPTA KEPSFTADGFEISVGTNHLGHFLLSRLLLEDLKKSDYPSKRLIIVGSITGNTNTLAGNVP PKANLGDLRGLAGGLTGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRYHEETGIT FASLYPGCIATTGLFREHIPLFRTLFPPFQKYITKGYVSEEESGKRLAQVVSDPSLTKSG VYWSWNNASASFENQLSQEASDAEKARKVWEVSEKLVGLA PIR:S14990 >P1;S14990 protochlorophyllide reductase (EC 1.3.1.33) precursor - Arabidopsis thaliana C;Species: Arabidopsis thaliana (mouse-ear cress) C;Date: 21-Nov-1993 #sequence_revision 12-May-1995 #text_change 01-Nov-1996 C;Accession: S14990 R;Benli, M.; Schulz, R.; Apel, K. Plant Mol. Biol. 16, 615-625, 1991 A;Title: Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana. A;Reference number: S14990; MUID:91329695 A;Accession: S14990 A;Status: nucleic acid sequence not shown; not compared with conceptual translation A;Molecule type: mRNA A;Residues: 1-401 C;Genetics: A;Genome: nuclear C;Keywords: chloroplast; NADP; oxidoreductase F;1-81/Domain: transit peptide (chloroplast) #status predicted F;82-401/Product: protochlorophyllide reductase #status predicted >S14990 MALQAASLVSSAFSVRKDAKLNASSSSFKDSSLFGASITDQIKSEHGSSSLRFKREQSLR NLAIRAQTAATSSPTVTKSVDGKKTLRKGNVVVTGASSGLGLATAKALAETGKWNVIMAC RDFLKAERAAKSVGMPKDSYTVMHLDLASLDSVRQFVDNFRRTETPLDVLVCNAAVYFPT AKEPTYSAEGFELSVATNHLGHFLLARLLLDDLKKSDYPSKRLIIVGSITGNTNTLAGNV PPKANLGDLRGLAGGLNGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRFHEETGV TFASLYPGCIASTGLFREHIPLFRALFPPFQKYITKGYVSETESGKRLAQVVSDPSLTKS GVYWSWNNASASFENQLSEEASDVEKARKVWEISDKLVGLA PIR:JC4146 >P1;JC4146 protochlorophyllide reductase (EC 1.3.1.33) - cucumber N;Alternate names: NADPH-protochlorophyllide oxidoreductase C;Species: Cucumis sativus (cucumber) C;Date: 31-Aug-1995 #sequence_revision 27-Oct-1995 #text_change 26-Jul-1996 C;Accession: JC4146 R;Kuroda, H.; Masuda, T.; Ohta, H.; Shioi, Y.; Takamiya, K. Biochem. Biophys. Res. Commun. 210, 310-316, 1995 A;Title: Light-enhanced gene expression of NADPH-protochlorophyllide oxidoreductase in cucumber. A;Reference number: JC4146 A;Accession: JC4146 A;Molecule type: mRNA A;Residues: 1-398 A;Experimental source: seed C;Comment: This enzyme catalyzes photoconversion of protochlorophyllide to chlorophyllide alpha and its expression is negatively regulated by light. C;Keywords: oxidoreductase F;1-63/Domain: (or 1-79) signal sequence #status predicted F;64-398/Product: (or 80-398) protochlorophyllide reductase #status predicted >JC4146 MALQAASLVSPALSIPKEGKSSVCLKDSSLFGISFSDHLKSEFSSSTLRCKRELNQQIGA IRAQTTATESPAVNKATPDGKKTLRKGSVVITGASSGLGLATAKALAETGKWHVIMACRD FLKAERAAKSAGITKENYTVMHLDLASLDSVRQFVDNFRQSGRPLDVLVCNAAVYLPTAK EPTFTAEGFELSVGTNHLGHFLLSRLLLEDLNKSSYPSKRLIIVGSITGNTNTLAGNVPP KANLGDLRGLAGGLNGLKSSMIDGGEFDGAKAYKDSKVCNMLTMQEFHKRYHEETGITFA SLYPGCIATTGLFREHIPLFRILFPPFQKFITQGYVSEDEAGKRLAQVVSEPSLTKSGVY WSWNKNSASFENQLSQEASDAEKARKVWELSEKLVGLA PIR:S30167 >P1;S30167 protochlorophyllide reductase (EC 1.3.1.33) precursor - loblolly pine C;Species: Pinus taeda (loblolly pine) C;Date: 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 C;Accession: S30167 R;Spano, A.J.; He, Z.; Timko, M.P. Mol. Gen. Genet. 236, 86-95, 1992 A;Title: NADPH: protochlorophyllide oxidoreductases in white pine (Pinus strobus) and loblolly pine (P. taeda). Evidence for light and developmental regulation of expression and conservation in gene organization and protein structure between angiosperms and gymnosperms. A;Reference number: S30167 A;Accession: S30167 A;Molecule type: DNA A;Residues: 1-400 A;Cross-references: EMBL:X66727 C;Genetics: A;Introns: 19/3; 52/3; 230/1; 349/3 C;Keywords: chloroplast; NADP; oxidoreductase F;1-66/Domain: transit peptide (chloroplast) #status predicted F;67-400/Product: protochlorophyllide reductase #status predicted >S30167 MGTLLQTHIGSVAFALQKEGGHSASAKDSAFLGVSLVEHGKKEFSFPVIRAKKVTSRNTN VPRIRAQTVAAPVETKEAPASKKTDRKGNVIITGASSGLGLATAKALGESGKWHIIMACR DFLKAERMARSVGIPKENYTVMHLDLASLESVRQFADNFRRSGRPLDVLVCNAAIYLPTA KLPTYTAEGFELSVGTNHLGHFLLSRLLLEDMKTSDFNSKRVIIVGSITGNTNTLAGNVP PKANLGDLRGLAGGLNGVNISPMIDGGEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGIT FASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGFVSEEEAGKRLAQVVSNPSLTKSG VYWSWNNNSASFENQLSEEASDPEKAKKLWEVSEKLVGLA PIR:A36904 >P1;A36904 protochlorophyllide reductase (EC 1.3.1.33) - Synechococcus sp. C;Species: Synechococcus sp. C;Date: 07-Apr-1994 #sequence_revision 12-Apr-1996 #text_change 12-Apr-1996 C;Accession: S25621; A36904 R;Lieman-Hurwitz, J.; Ronen-Tarazi, M.; Gabai, C.; Hassidim, M.; Schwarz, R.; Kaplan, A. submitted to the EMBL Data Library, August 1992 A;Reference number: S25616 A;Accession: S25621 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-466 A;Cross-references: EMBL:X67694 R;Price, G.D.; Howitt, S.M.; Harrison, K.; Badger, M.R. J. Bacteriol. 175, 2871-2879, 1993 A;Title: Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp. strain PCC7942 involved in carboxysome assembly and function. A;Reference number: A36904; MUID:93259930 A;Accession: A36904 A;Status: preliminary A;Molecule type: DNA A;Residues: 388-466 A;Cross-references: NCBIN:131726; NCBIP:131727 A;Experimental source: PCC 7942 A;Note: sequence extracted from NCBI backbone C;Keywords: oxidoreductase >A36904 MTTTEAPSALSFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMI FAEPRYAMAELEEGDISAQLNDYAELKRLCTQIKRDRNPSVIVWIGTCTTEIIKMDLEGL APKLEAEIGIPIVVARANGLDYAFTQGEDTVLAAMAARCPEAATSEADQQERTNAIQRLL QFGKSPAAEQQPASSKHPPLILFGSVPDPVATQLTIELAKQGITVSGWLPAKRYTELPVI AEGSYAIGLNPFLSRTATTLMRRRKCKVIGAPFPIGPDGSRAWIEKICSVLEIEPQGLAE REAQVWDSIEDYRQLVEGKQVFFMGDNLWEISLARFLVRCGMRCPEIGIPYLDRRYLGAE LAMLEATCQSMGVPLPRLVEKPDNYNQLQRIEALQPDLVITGMAHANPLEARGISTKWSV EFTFAQIHGFGNARAILELVTRPLRRNLALGTLGGSQWVSEAVTSR PIR:C49851 >P1;C49851 protochlorophyllide reductase (EC 1.3.1.33) 57K chain - Rhodobacter capsulatus N;Alternate names: chlorin reductase subunit bchB C;Species: Rhodobacter capsulatus C;Date: 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 17-Nov-1995 C;Accession: C49851; S17809 R;Burke, D.H.; Alberti, M.; Hearst, J.E. J. Bacteriol. 175, 2414-2422, 1993 A;Title: bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants. A;Reference number: A49851; MUID:93224465 A;Accession: C49851 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-525 A;Cross-references: NCBIN:129238; NCBIP:129241; EMBL:Z11165 A;Experimental source: SB1003 A;Note: sequence extracted from NCBI backbone C;Genetics: A;Gene: bchB C;Keywords: oxidoreductase >C49851 MKLTLWTYEGPPHVGAMRVATAMKDLQLVLHGPQGDTYADLLFTMIERRNARPPVSFSTF EASHMGTDTAILLKDALAAAHARYKPQAMAVALTCTAELLQDDPNGISRALNLPVPVVPL ELPSYSRKENYGADETFRALVRALAVPMERTPEVTCNLLGATALGFRHRDDVAEVTKLLA TMGIKVNVCAPLGASPDDLRKLGQAHFNVLMYPETGESAARHLERACKQPFTKIVPIGVG ATRDFLAEVSKITGLPVVTDESTLRQPWWSASVDSTYLTGKRVFIFGDGTHVIAAARIAA KEVGFEVVGMGCYNREMARPLRTAAAEYGLEALITDDYLEVEKAIEAAAPELILGTQMER NIAKKLGLPCAVISAPVHVQDFPARYAPQMGFEGANVLFDTWVHPLVMGLEEHLLTMFRE DFEFHDAAGASHHGGKAVAREESPVAPADLAPAATSDTPAAPSPVVVTQASGEIRWMPEA ERELRKIPFFVRGKAKRNTELYAAHKGVCDITVETLYEAKAHYAR PIR:D49850 >P1;D49850 protochlorophyllide reductase (EC 1.3.1.33) 53K chain - Rhodobacter capsulatus N;Alternate names: chlorin reductase subunit bchZ C;Species: Rhodobacter capsulatus C;Date: 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 17-Nov-1995 C;Accession: D49850; S17825 R;Burke, D.H.; Alberti, M.; Hearst, J.E. J. Bacteriol. 175, 2407-2413, 1993 A;Title: The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA, consists of three genes, bchX, bchY, and bchZ. A;Reference number: A49850; MUID:93224464 A;Accession: D49850 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-490 A;Cross-references: NCBIN:129230; NCBIP:129234; EMBL:Z11165 A;Experimental source: strain SB1003 A;Note: sequence extracted from NCBI backbone C;Genetics: A;Gene: bchZ C;Keywords: oxidoreductase >D49850 MFLLDHDRAGGYWGAVYTFCAVKGLQVVIDGPVGCENLPVTSVLHYTDGLPPHELPIVVT GLGDAELGREGTEGAMSRAWKTLDPLLPSVVVTGSIAEMIGGGVTPQGTNLQRFLARTID EDQWQCADRAMTWLFTEYGMTKGRMPGERMRPDGAKPRVNILGPMYGAFNMASDLHEIRR LVEGIGAEVNMVFPLGTHLSEVRNLVNADVNVVMYREFGRNLAEILGKPYLQAPIGLEST TKFLRSLGELLGLDPEPFIEREKHATLKPLWDLWRSVTQDFFATASFGICATETYARGIK AYLEGDLGLPCAFAVARKAGEKTKSDEVRGLIRQTRPLVVFGSINEKIYLAETKAGHGPA ASFVPASFPGAAIRRATGTPFMGYMGSVYLLQEICNGLFDALFNILPLASEMDSAAATPA TLRRDMPWDADAQAALDRIVSQHPVLTRISAAKSLRDAAEKAALDQGAERVVLEMVEALG DATMDRKGGN PIR:C49850 >P1;C49850 protochlorophyllide reductase (EC 1.3.1.33) 52.5K chain - Rhodobacter capsulatus N;Alternate names: chlorin reductase subunit bchY C;Species: Rhodobacter capsulatus C;Date: 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 17-Nov-1995 C;Accession: C49850; S17824 R;Burke, D.H.; Alberti, M.; Hearst, J.E. J. Bacteriol. 175, 2407-2413, 1993 A;Title: The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA, consists of three genes, bchX, bchY, and bchZ. A;Reference number: A49850; MUID:93224464 A;Accession: C49850 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-497 A;Cross-references: NCBIN:129230; NCBIP:129233; EMBL:Z11165 A;Experimental source: strain SB1003 A;Note: sequence extracted from NCBI backbone C;Genetics: A;Gene: bchY C;Keywords: oxidoreductase >C49850 MTDLPQAEGGCGAGNERLAAQAAAAGNAELMARFKADYPVGPHDKPQTMCPAFGALRVGL RMRRVATVLCGSACCVYGLSFISHFYGARRSVGYVPFDSETLVTGKLFEDVRASVHDLAD PARYDAIVVINLCVPTASGVPLQLLPNEINGVRVVGIDVPGFGVPTHAEAKDVLSGAMLA YARQEVMAGPVPAPISGRSDRPTVTLLGEMFPADPMVIGAMLAPMGLAVGPTVPMRDWRE LYAALDSKVVAAIHPFYTAAIRQFEAAGRAIVGSAPVGHDGTMEWLANIGRAYDVSPDKI AAAQNAFGPAIRGAIAGAPIKGRITVSGYEGSELLVARLLIESGAEVPYVGTAAPRTPWS AWDKDWLESRGVVVKYRASLEDDCAAMEGFEPDLAIGTTPLVQKAKALGIPALYFTNLIS ARPLMGPAGAGSLAQVMNAAMGNRERMGKMKAFFEGVGEGDTAGIWQDTPKLYPDFREQQ RKKMEKAAKLAKAEEMI PIR:B49851 >P1;B49851 protochlorophyllide reductase (EC 1.3.1.33) 46K chain - Rhodobacter capsulatus N;Alternate names: chlorin reductase subunit bchN C;Species: Rhodobacter capsulatus C;Date: 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 17-Nov-1995 C;Accession: B49851; S17810 R;Burke, D.H.; Alberti, M.; Hearst, J.E. J. Bacteriol. 175, 2414-2422, 1993 A;Title: bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants. A;Reference number: A49851; MUID:93224465 A;Accession: B49851 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-424 A;Cross-references: NCBIN:129238; NCBIP:129240; EMBL:Z11165 A;Experimental source: SB1003 A;Note: sequence extracted from NCBI backbone C;Genetics: A;Gene: bchN C;Keywords: oxidoreductase >B49851 MSLDSPTFGCTDSPVRRERGQKAVFCGLTSIVWLHRKMQDAFFLVVGSRTCAHLLQAAAG VMIFAEPRFGTAVLEEQDLAGLADAHKELDREVAKLLERRPDIRQLFLVGSCPSEVLKLD LDRAAERLSGLHAPHVRVYSYTGSGLDTTFTQGEDTCLAAMVPTLDTTEAAELIVVGALP DVVEDQCLSLLTQLGVGPVRMLPARRSDIEPAVGPNTRFILAQPFLGETTGALERRGAKR IAAPFPFGEEGTTLWLKAVADAYGVSAEKFEAVTAAPRARAKKAIAAHLETLTGKSLFMF PDSQLEIPLARFLARECGMKTTEIATPFLHKAIMAPDLALLPSNTALTEGQDLEAQLDRH EAINPDLTVCGLGLANPLEAKGHATKWAIELVFTPVHFYEQAGDLAGLFSRPLRRRALLN GGAA PIR:S17823 >P1;S17823 protochlorophyllide reductase (EC 1.3.1.33) 35.5K chain - Rhodobacter capsulatus N;Alternate names: chlorophyll Fe protein C;Species: Rhodobacter capsulatus C;Date: 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 28-Apr-1993 C;Accession: S17823 R;Burke, D.H.; Alberti, M.; Armstrong, G.A.; Hearst, J.E. submitted to the EMBL Data Library, November 1991 A;Description: The complete nucleotide sequence of the 46 kb photosynthesis gene cluster of Rhodobacter capsulatus. A;Reference number: S17803 A;Accession: S17823 A;Molecule type: DNA A;Residues: 1-333 A;Cross-references: EMBL:Z11165 C;Genetics: A;Gene: bchX C;Keywords: oxidoreductase >S17823 MTDAPNLKGFDARLREEAAEEPTLEIPEQPPTKKTQIIAIYGKGGSGKSFTLANLSHMMA EMGKRVLLIGCDPKSDTTSLLFGGKNCPTIIETATKKKLAGEEVKVGDVCFKSGGVFAME LGGPEVGRGCGGRGIIHGFELLEKLGFHDWDFDFVLLDFLGDVVCGGFGLPIARDMAQKV IVIGSNDLQSLYVANNVCNAVEYFRKLGGNVGVAGIVINKDDGTGEAQAFAREVGIPILA AIPADEELRRKSAAYQIVGSHATPWGKLFEELAGNVADAPPLRPRPLSPDALLALFETDE ETRVVDLVPATDEDLRGSNAAPKKSLEVIYDDV SWISSPROT:PCR_PEA ID PCR_PEA STANDARD; PRT; 399 AA. AC Q01289; DT 01-APR-1993 (REL. 25, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-APR-1993 (REL. 25, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE PRECURSOR (EC 1.3.1.33) (PCR) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). GN 3PCR. OS PISUM SATIVUM (GARDEN PEA). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 65-76. RC STRAIN=CV. PROGRESS NO. 9; RX MEDLINE; 92256817. RA SPANO A.J., HE Z., MICHEL H., HUNT D.F., TIMKO M.P.; RL PLANT MOL. BIOL. 18:967-972(1992). CC -!- FUNCTION: THE FIRST STEP OF TRANSFORMATION OF ETIOPLASTS TO CC PROTOPLASTS, MEDIATED BY LIGHT, IS THE PHOTOTRANSFORMATION OF CC PROTOCHLOROPHYLLIDE TO CHLOROPHYLLIDE. THIS REACTION IS CC CATALYZED BY PCR. CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- SUBCELLULAR LOCATION: PROLAMELLAR BODY OF ETIOLATED SEEDLING. DR EMBL; X63060; G20830; -. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 64 CHLOROPLAST. FT CHAIN 65 399 NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE. SQ SEQUENCE 399 AA; 42962 MW; 95C1FA3C CRC32; >PCR_PEA MALQTASMLPASFSIPKEGKIGASLKDSTLFGVSSLSDSLKGDFTSSALRCKELRQKVGA VRAETAAPATPAVNKSSSEGKKTLRKGNVVITGASSGLGLATAKALAESGKWHVIMACRD YLKAARAAKSAGLAKENYTIMHLDLASLDSVRQFVDNFRRSEMPLDVLINNAAVYFPTAK EPSFTADGFEISVGTNHLGHFLLSRLLLEDLKKSDYPSKRLIIVGSITGNTNTLAGNVPP KANLGDLRGLAGGLTGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITF ASLYPGCIATTGLFREHIPLFRTLFPPFQKYITKGYVSEEESGKRLAQVVSDPSLTKSGV YWSWNNASASFENQLSQEASDAEKARKVWEVSEKLVGLA SWISSPROT:PCR_HORVU ID PCR_HORVU STANDARD; PRT; 388 AA. AC P13653; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-AUG-1992 (REL. 23, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE PRECURSOR (EC 1.3.1.33) (PCR) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=CV. CARINA; TISSUE=LEAF; RX MEDLINE; 89364719. RA SCHUELZ R., STEINMUELLER K., KLAAS M., FORREITER C., RASMUSSEN S., RA HILLER C., APEL K.; RL MOL. GEN. GENET. 217:355-361(1989). CC -!- FUNCTION: THE FIRST STEP OF TRANSFORMATION OF ETIOPLASTS TO CC PROTOPLASTS, MEDIATED BY LIGHT, IS THE PHOTOTRANSFORMATION OF CC PROTOCHLOROPHYLLIDE TO CHLOROPHYLLIDE. THIS REACTION IS CC CATALYZED BY PCR. CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- SUBCELLULAR LOCATION: PROLAMELLAR BODY OF ETIOLATED SEEDLING. CC -!- SIMILARITY: 95% TO PCR OF ARABIDOPSIS THALIANA. DR EMBL; X15869; G19061; -. DR PIR; S04783; S04783. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 74 CHLOROPLAST. FT CHAIN 75 388 NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE. SQ SEQUENCE 388 AA; 41181 MW; 5B470928 CRC32; >PCR_HORVU MALQLLPSTLSVPKKGSSMGAVAVKDTAAFLGVSSKAKKASLAVRTQVATAPSPVTTSPG STASSPSGKKTLRQGVVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAG MADGSYTVMHLDLASLDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARTPTFTADGHEMS VGVNHLGHFLLARLLMEDLQKSDYPSRRMVIVGSITGNSNTLAGNVPPKASLGDLRGLAG GLSGASGSAMIDGDESFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFSSLYPGCIATT GLFREHIPLFRTLFPPFQKFVTKGFVSEAESGKRLAQVVAEPVLTKSGVYWSWNKDSASF ENQLSQEASDPEKARKVWELSEKLVGLA SWISSPROT:PCR_AVESA ID PCR_AVESA STANDARD; PRT; 313 AA. AC P15904; DT 01-APR-1990 (REL. 14, CREATED) DT 01-APR-1990 (REL. 14, LAST SEQUENCE UPDATE) DT 01-AUG-1992 (REL. 23, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE (EC 1.3.1.33) (PCR) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE) (FRAGMENT). OS AVENA SATIVA (OAT). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. PENIARTH; TISSUE=ETIOLATED LEAF; RX MEDLINE; 90165879. RA DARRAH P.M., KAY S.A., TEAKLE G.R., GRIFFITHS W.T.; RL BIOCHEM. J. 265:789-798(1990). CC -!- FUNCTION: THE FIRST STEP OF TRANSFORMATION OF ETIOPLASTS TO CC PROTOPLASTS, MEDIATED BY LIGHT, IS THE PHOTOTRANSFORMATION OF CC PROTOCHLOROPHYLLIDE TO CHLOROPHYLLIDE. THIS REACTION IS CC CATALYZED BY PCR. CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- SUBCELLULAR LOCATION: PROLAMELLAR BODY OF ETIOLATED SEEDLING. DR EMBL; X17067; G829253; -. DR PIR; S08406; S08406. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP; KW CHLOROPLAST. FT NON_TER 1 1 SQ SEQUENCE 313 AA; 33796 MW; D9C0EC56 CRC32; >PCR_AVESA VVVITGASSGLGLAAAKALAETGKWHVVMACRDFLKASKAAKAAGMADGSYTVMHLDLAS LDSVRQFVDAFRRAEMPLDVLVCNAAIYRPTARKPTFTAEGVEMSVGVNHLGHFLLARLL LEDLQKSDYPSRRLVIVGSITGNDNTLAGNVPPKANLGDLRGLAGGLTGASGSAMIDGDE SFDGAKAYKDSKVCNMLTMQEFHRRYHEDTGITFSSLYPGCIATTGLFREHIPLFRTLFP PFQKFVTKGFVSEAESGKRLAQVVGEPSLTKSGVYWSWNKDSASFENQLSQEASDPEKAR KVWELSEKLVGLA SWISSPROT:PCR_ARATH ID PCR_ARATH STANDARD; PRT; 401 AA. AC P21218; DT 01-MAY-1991 (REL. 18, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-JUL-1993 (REL. 26, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE PRECURSOR (EC 1.3.1.33) (PCR) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=CV. ANTWERPEN 2; TISSUE=LEAF; RX MEDLINE; 91329695. RA BENLI M., SCHUELZ R., APEL K.; RL PLANT MOL. BIOL. 16:615-625(1991). CC -!- FUNCTION: THE FIRST STEP OF TRANSFORMATION OF ETIOPLASTS TO CC PROTOPLASTS, MEDIATED BY LIGHT, IS THE PHOTOTRANSFORMATION OF CC PROTOCHLOROPHYLLIDE TO CHLOROPHYLLIDE. THIS REACTION IS CC CATALYZED BY PCR. CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- SUBCELLULAR LOCATION: PROLAMELLAR BODY OF ETIOLATED SEEDLING. CC -!- SIMILARITY: 95% TO PCR OF BARLEY. DR PIR; S14990; S14990. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 81 CHLOROPLAST (POTENTIAL). FT CHAIN 82 401 NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE. SQ SEQUENCE 401 AA; 43345 MW; 6F670704 CRC32; >PCR_ARATH MALQAASLVSSAFSVRKDAKLNASSSSFKDSSLFGASITDQIKSEHGSSSLRFKREQSLR NLAIRAQTAATSSPTVTKSVDGKKTLRKGNVVVTGASSGLGLATAKALAETGKWNVIMAC RDFLKAERAAKSVGMPKDSYTVMHLDLASLDSVRQFVDNFRRTETPLDVLVCNAAVYFPT AKEPTYSAEGFELSVATNHLGHFLLARLLLDDLKKSDYPSKRLIIVGSITGNTNTLAGNV PPKANLGDLRGLAGGLNGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRFHEETGV TFASLYPGCIASTGLFREHIPLFRALFPPFQKYITKGYVSETESGKRLAQVVSDPSLTKS GVYWSWNNASASFENQLSEEASDVEKARKVWEISDKLVGLA SWISSPROT:CHLN_SYNY3 ID CHLN_SYNY3 STANDARD; PRT; 469 AA. AC P28372; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE 46 KD CHAIN (EC 1.3.1.33) (ORF 469). GN CHLN. OS SYNECHOCYSTIS SP. (STRAIN PCC 6803). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92330029. RA OGURA Y., TAKEMURA M., ODA K., YAMATO K., OHTA E., FUKUZAWA H., RA OHYAMA K.; RL BIOSCI. BIOTECHNOL. BIOCHEM. 56:788-793(1992). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; D10474; G217094; -. DR PIR; JT0601; JT0601. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 469 AA; 52474 MW; E4F4EDC3 CRC32; >CHLN_SYNY3 MTVAQQAPSALNFDCETGNYHTFCPISCVSWLYQKIEDSFFLVIGTKTCGYFLQNAMGVM IFAEPRYAMAELEEGDISAQLKDYEELKRLCLQIKRDRNPSVIVWIGTCTTEIIKMDLEG LAPQLEAEIGIPIVTARANGLDYAFTQGEDTVLASMAHKCPTSAQVQGEDKEERNAIQKL LTFGRKADQEKVESEYVDHQPLVLFGSLPDPVVTNLTLELKKQGVKVSGWLPAKRYTELP VIDEGYYVAGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVLGIEPQGL EEREAQIWASLEDYIQLIRGKSVFFMGDNLLEVSLARFLIRCGMTCPEIGIPYMDKRYQA AELALLEKTCSDMGVPLPNIVEKPDNYNQIQRIKALQPDLVITGMAHANPLEAQGINTKW SVEFTFAQIHGFTNARDILELATRPLRRNSQLGELGWDKLIAKDVPAQV SWISSPROT:CHLN_SYNP7 ID CHLN_SYNP7 STANDARD; PRT; 466 AA. AC P54208; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE 46 KD CHAIN (EC 1.3.1.33) (ORF466). GN CHLN. OS SYNECHOCOCCUS SP. (STRAIN PCC 7942) (ANACYSTIS NIDULANS R2). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RA LIEMAN-HURWITZ J., RONEN-TARAZI M., GABAI C., HASSIDIM M., RA SCHWARZ R., KAPLAN A.; RL SUBMITTED (SEP-1992) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; X67694; G46847; -. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 466 AA; 51540 MW; A5D97FFB CRC32; >CHLN_SYNP7 MTTTEAPSALSFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMI FAEPRYAMAELEEGDISAQLNDYAELKRLCTQIKRDRNPSVIVWIGTCTTEIIKMDLEGL APKLEAEIGIPIVVARANGLDYAFTQGEDTVLAAMAARCPEAATSEADQQERTNAIQRLL QFGKSPAAEQQPASSKHPPLILFGSVPDPVATQLTIELAKQGITVSGWLPAKRYTELPVI AEGSYAIGLNPFLSRTATTLMRRRKCKVIGAPFPIGPDGSRAWIEKICSVLEIEPQGLAE REAQVWDSIEDYRQLVEGKQVFFMGDNLWEISLARFLVRCGMRCPEIGIPYLDRRYLGAE LAMLEATCQSMGVPLPRLVEKPDNYNQLQRIEALQPDLVITGMAHANPLEARGISTKWSV EFTFAQIHGFGNARAILELVTRPLRRNLALGTLGGSQWVSEAVTSR SWISSPROT:CHLN_PORPU ID CHLN_PORPU STANDARD; PRT; 435 AA. AC P51188; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33). GN CHLN. OS PORPHYRA PURPUREA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; RHODOPHYTA (RED ALGAE). RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AVONPORT; RA REITH M.E., MUNHOLLAND J.; RL PLANT MOL. BIOL. REP. 13:333-335(1995). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; U38804; G1276654; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 435 AA; 49181 MW; 65B183A3 CRC32; >CHLN_PORPU MSIVQSDALTFECETGNYHTFCPISCVSWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIF AEPRYAMAELEEGDISAKLNDYGELRRLCLQIKKDRNPSVIFWIGTCTTEIIKMDLEGIA PKLEAEIRVPIVVARANGLDYAFTQGEDTVLAAMAQRCPSHHYIENTNPHVPLVLFGSLP DPVVTQLVMELKKQGIIVSGWLPSKRYTELPVIQEGYYVAGVNPFLSRTATTLMRRRKTK LIGAPFPIGPDGTRAWIEKICSVFSIKPEGLAEREKDIWDSLEDYIALIRGKSVFFMGDN LLEVSLARFLTRCGMTVYEIGIPYMDKRYQAAELALLKSTCDDMNVMMPTIVEKPDNYNQ LDRIRDLKPDLVITGMAHANPLEARGINTKWSVEFTFAQIHGFTNARDILELVTRPLRRN LSLSELGWDIYSKQG SWISSPROT:CHLN_PLEBO ID CHLN_PLEBO STANDARD; PRT; 467 AA. AC Q04607; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE 46 KD CHAIN (EC 1.3.1.33) (ORF467). GN CHLN. OS PLECTONEMA BORYANUM. OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); NOSTOCALES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=IAM-M101; RX MEDLINE; 94258400. RA FUJITA Y., MATSUMOTO H., TAKAHASHI Y., MATSUBARA H.; RL PLANT CELL PHYSIOL. 34:305-314(1993). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; D12973; G216812; -. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 467 AA; 52795 MW; 9740F18A CRC32; >CHLN_PLEBO MTLADAQPQALNFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVM IFAEPRYAMAELEEGDISAQLNDYNELKRLCEQIKRDRNPSVIVFIGTCTTEIIKMDLEG LAPKLESEIGIPIVVARANGLDYAFTQGEDTVLAAMAQRCPTQAPTAEADKEERNAIQKL MNFGRKQEDVKREESEYVDHPPLVMFGSVPDPIVTQLSLELKHQGIKVSGWLPAKRYTEL PVIEEGYYVSGVNPFLSRTATTLMRRRKAKLIGSPFPIGPDGTRAWVEKICSVFNIEPKG LEEREAKIWQSVEDYLQLIRGKSVFFMGDNLLEISLARFLIRCGMTCHEIGIPYMDKRYQ AAELDFLVKTCQEMGVPVPTIVEKPDNYNQLQRIHELKPDLVITGMAHANPLEARGISTK WSVEFTFAQIHGFGNTRDILELVTRPLRRNGALKDLGWEKLVEEARV SWISSPROT:CHLN_PINTH ID CHLN_PINTH STANDARD; PRT; 467 AA. AC P41646; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33). GN CHLN. OS PINUS THUNBERGII (GREEN PINE) (JAPANESE BLACK PINE). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95024047. RA WAKASUGI T., TSUDZUKI J., ITO S., NAKASHIMA K., TSUDZUKI T., RA SUGIURA M.; RL PROC. NATL. ACAD. SCI. U.S.A. 91:9794-9798(1994). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; D17510; G1262726; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 467 AA; 53012 MW; C3D2A03D CRC32; >CHLN_PINTH MSTKIVETITLECETGNYHSFCPISCVSWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIF AEPRYAMAELEEGDISAHLNDYEELKTLCIRIRKDRDPSVIIWIGTCTTEIIKMDLEGMA PKLEYEIGVPILVARANGLDYAFTQGEDTVLAVMAHRCPDQELPIGESKETKTKLFPFPL LKEKNLVEYANHPPLVIFGSLPSNLVSQLDTELRRQFIKVSGWLPAQRYADLPSLGDGVY VCGVNPFLSRTATTLIRRKKCELIVAPFPIGPDGTRAWIERICPVFGIEAQSLEEREERI WESLKDYLDLVRGKSVFFMGDNLIEISIARFLIRCGMIVYEIGIPYMDKRYQAAELALLQ NTCIRMCMPIPRIVEKPDNSNQIRRMRELQPDLAITGMAHANPLGARGIGTKWSVEFTFA QIHGFANARDVLELVTRPLRRNENLDNLDRTTLVRKNNELYTSTPVK SWISSPROT:CHLN_PINCO ID CHLN_PINCO STANDARD; PRT; 459 AA. AC P26180; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33). GN CHLN OR GIDA. OS PINUS CONTORTA (SHORE PINE) (LODGEPOLE PINE). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEAF; RX MEDLINE; 92003690. RA LIDHOLM J., GUSTAFSSON P.; RL PLANT MOL. BIOL. 17:787-798(1991). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; X56200; G12089; -. DR PIR; S17742; S17742. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 459 AA; 52121 MW; 3A6B3552 CRC32; >CHLN_PINCO MSTKIVETITLECETGNYHSFCPISCVSWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIF AEPRYAMAELEEGDISAHLNDYEELKTLCIRIRKDRDPSVIIWIGTCTTEIIKMDLEGMA PKLEYEIGVPILVARANGLDYAFTQGEDTVLAVMAHRCPDQEFPIGESKETKKKLFPFPL LKENNLVEYANHPPLVIFGSLPSNLVSQLDTELRRQFIKVSGWLPAQRYADLPSLGDGVY VCGVNPFLSRTATTLIRRKKCELIVAPFPIGPDGTRAWIERICPVFGIEAQSLEEIEERI WESLKDYLDLVRGKSVFFMGDNLIEISIARFLIRCGMIVYEIGIPYLDKRYQAAELALLK KTCIRMCMPIPRIVEKPDNSNQIRRMRELKPDLAITGMAHANPLGARGIGTKWSVEFTFA QIHGFANARDVLELVTRPLRRNENLDNLDRTTLVRKNNK SWISSPROT:CHLN_MARPO ID CHLN_MARPO STANDARD; PRT; 465 AA. AC P26156; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33) (ORF 465). GN CHLN. OS MARCHANTIA POLYMORPHA (LIVERWORT). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; HEPATICOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA OHYAMA K.; RL SUBMITTED (OCT-1986) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP COMPLETE GENOME. RA OHYAMA K., FUKUZAWA H., KOHCHI T., SHIRAI H., SANO T., SANO S., RA UMESONO K., SHIKI Y., TAKEUCHI M., CHANG Z., AOTA S., INOKUCHI H., RA OZEKI H.; RL NATURE 322:572-574(1986). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE; 89068688. RA KOHCHI T., SHIRAI H., FUKUZAWA H., SANO T., KOMANO T., UMESONO K., RA INOKUCHI H., OZEKI H., OHYAMA K.; RL J. MOL. BIOL. 203:353-372(1988). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; X04465; -; NOT_ANNOTATED_CDS. DR PIR; S01518; S01518. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 465 AA; 53097 MW; 3E945070 CRC32; >CHLN_MARPO MSIKISETLTFECETGNYHTFCPISCVAWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIF AEPRYAMAELEEGDISAQLNDYEELKRLCVQIKKDRNPSVIIWIGTCTTEIIKMDLEGMA PKLENEIEIPIVVARANGLDYAFTQGEDTVLAAMAHRCPEQKTEIEKKIDDKSIQELFSF LPLKTKEKSNKSFTLKNTFSLVLFGSLPSTVASQLSLELKRQSIHVSGWLPAQRYTDLPI LGDKVYVCGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVFNIETQGLE EREQQVWESLKNYLNLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYMDKRYQAA ELTLLQETCKKMCIPMPRIVEKPDNYNQIQRMRELQPDLAITGMAHANPLEARGINTKWS VEFTFAQIHGFTNAKDVLELVTRPLRRNNNLENLGWTNLIKIQKR SWISSPROT:CHLN_CYAPA ID CHLN_CYAPA STANDARD; PRT; 460 AA. AC P48100; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33). GN CHLN. OS CYANOPHORA PARADOXA. OG CYANELLE. OC EUKARYOTA; PLANTA; PHYCOPHYTA; GLAUCOPHYTA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LB555 / PRINGSHEIM; RA STIREWALT V.L., MICHALOWSKI C.B., LUFFELHARDT W., BOHNERT H.J., RA BRYANT D.A.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR EMBL; U30821; G1016230; -. KW CYANELLE; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 460 AA; 52449 MW; 7A48C8C1 CRC32; >CHLN_CYAPA MNQINNSTLTFQCETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNSMGVMIF AEPRYAMAELEEGDISAQINDYEELKRLCTQIKNDRNPSVIVFIGTCTTEIIKMDLEGIA PKLEAEIGIPIVVARANGLDYTFTQGEDTVLASLIQRCPSKDRETEKINKNNSSLFPSLS IFSKNKNESNLSQDKPNLPLVLFGSLPNSLTNQLEHELEKQNIKISGWLPTKNYKELPVI HEGDYVCGVNPYLARTATNLIRRRKCKLISAPFPIGPDGTRAWIEKICSIFNIEPTGLDE REKAVWDSLENYLPLVKGKSVFFMGDNLLELSIARFLIRCGMIVPEIGIPYLHKRYQEAE IKLLEDTCRKMQVPTPLIIEKPDNYEELKRIEQYRPDLVITGMANANPLEARGINTKWSV EFTFAQIHGFSNARDILELVTRSLRRKNYIQQLGWKELVE SWISSPROT:CHLN_CHLRE ID CHLN_CHLRE STANDARD; PRT; 545 AA. AC P29683; DT 01-APR-1993 (REL. 25, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLN SUBUNIT (EC 1.3.1.33). GN CHLN. OS CHLAMYDOMONAS REINHARDTII. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92258378. RA CHOQUET Y., RAHIRE M., GIRARD-BASCOU J., ERICKSON J., ROCHAIX J.-D.; RL EMBO J. 11:1697-1704(1992). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHN. DR PIR; S20968; S20968. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 545 AA; 60868 MW; CB6A169E CRC32; >CHLN_CHLRE MKPLKLKRLIMENNKSHATNLSLGGPFQGNCMPINQYFSKNQPNRGSSSSEKRSSLLPLW ESKNAADGFSIVSHNVLLDGATTILNLNSFFECETGNYHTFCPISCVAWLYQKIEDSFFL VIGTKTCGYFLQNALGVMIFAEPRYAMAELEESDISAQLNDYKELKRLCLQIKQDRNPSV IVWIGTCTTEIIKMDLEGMAPRLETEIGIPIVVARANGLDYAFTQGEDTVLSAMALASLK KDVPFLVGNTGLTNNQLLLEKSTSSVNGTDGKELLKKSLVLFGSVPSTVTTQLTLELKKE GINVSGWLPSANYKDLPTFNKDTLVCGINPFLSRTATTLMRRSKCTLICAPFPIGPDGTR VWIEKICGAFGINPSLNPITGNTNLYDREQKIFNGLEDYLKLLRGKSVFFMGDNLLEISL ARFLTRCGMIVYEIGIPYLDKRFQAAELALLEQTCKEMNVPMPRIVEKPDNYYQIRRIRE LKPDLTITGMAHANPLEARGITTKWSVEFTFAQIHGFTNTREILELVTQPLRRNLMSNQS VNAIS SWISSPROT:CHLB_ZAMFI ID CHLB_ZAMFI STANDARD; PRT; 103 AA. AC P37857; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS ZAMIA FISCHERI. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; GYMNOSPERMAE; CYCADALES. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25778; G495093; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11839 MW; DE1314D4 CRC32; >CHLB_ZAMFI RRLLRDLNIKINQVIPEGGSVKDLKNLPKAWFNLVPYREVGLMTAMYLEKKFGMPYVSTT PMGVVDMAECIQQIQRSVNTLAPTSSNKKVDYEPYIDEQTRFV SWISSPROT:CHLB_SELMO ID CHLB_SELMO STANDARD; PRT; 103 AA. AC P37856; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS SELAGINELLA MOLLIS (MOSS). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; LYCOPODIOPHYTA; ISOETOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25777; G495087; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11652 MW; 3839E407 CRC32; >CHLB_SELMO KRSSRDIGTRINQIIPEGEFVGNLNDLPKARFNFVPHREVGLMTAVYLDEEFGMPCISTT PAGIIDTAECIRQMQERVGKWASAPPKEKVDHEPYIDQHTRSV SWISSPROT:CHLB_SALAU ID CHLB_SALAU STANDARD; PRT; 103 AA. AC P37855; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS SALVINIA AURICULATA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; FILICOPHYTA; SALVINIALES. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25775; G495091; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11770 MW; A679A161 CRC32; >CHLB_SALAU KRSLRDLGILVNQIIPEGGSLKCLKDLPRAWFNVVPYREVGLMTAIFLEKEYGMPYVSVT PMGILDTAEFVRQMERLVNAWASVLPEKQANYSSYIKDQTNFV SWISSPROT:CHLB_PORPU ID CHLB_PORPU STANDARD; PRT; 507 AA. AC P51278; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS PORPHYRA PURPUREA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; RHODOPHYTA (RED ALGAE). RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AVONPORT; RA REITH M.E., MUNHOLLAND J.; RL PLANT MOL. BIOL. REP. 13:333-335(1995). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; U38804; G1276744; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 507 AA; 57288 MW; 24DDB689 CRC32; >CHLB_PORPU MKLAYWMYAGPAHIGTLRVASSFKKVHAIMHAPLGDDYFNVMRSMLERDRDFTPVTASVV DRHVLARGSQEKVVENITRKDREEKPDLVILTPTCTSSILQEDLQNFVSRASIETEADVL LADVNHYRVNELQASDRTLEQIVTFYMEKAKSNNILTKKTIKPSVNIIGAVSLGFHNQHD IAELKRLFHDLDIQINQVIPENASVHDLKNLPSAWFNFVPYRETGLMTALYLKKEFNMPY IDITPMGIVQTATSIRSIQKILNALGATVNYEKYIDEQTRFISQSAWFSRSIDCQNLTGK KAIVFGDATHAAAITRILHQEMGIHVAWCGTYCKYDEEWFREQVKGFCDEVIISDDHGLI GDLIAKTEPAAIFGTQMERHIGKRLNIPCGVISSPVHIQNFPLSYRPFLGYEGTNQIADL VYNSFTLGMEDHLLEIFGGHDTTEALSVGISADDSLNWSDEAQKELSKIPGFVRGKVKRN TEKFARDCSKNLITLELMYEAKEKVSS SWISSPROT:CHLB_POLCU ID CHLB_POLCU STANDARD; PRT; 100 AA. AC P37852; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS POLYTRICHUM COMMUNE (MOSS). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; BRYOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25772; G495062; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 100 100 SQ SEQUENCE 100 AA; 11573 MW; ADD74D48 CRC32; >CHLB_POLCU KRLLQDLNIKINQVIPEGGSVQDLQNLPKAWFNLVPYREVGLMTAIYLEKNFGMPYISTT PMGIVDIAECIRQIQKHVNNLALNQTFNYESYIDQQTRFV SWISSPROT:CHLB_PLESC ID CHLB_PLESC STANDARD; PRT; 100 AA. AC P37854; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS PLEUROZIUM SCHREBERI (MOSS). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; BRYOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25774; G495064; -. DR HSSP; P11347; 1MIO. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 100 100 SQ SEQUENCE 100 AA; 11659 MW; 3AE15A97 CRC32; >CHLB_PLESC KRLLQDLNIKVNKVIPEGGSVKDLQDLPKAWFNLVPYREIGLMTAIYLEKNFGMPYISIT PMGIVDTAEFIRQIEKHVNNLVSNKKFNYEPYIDQQTRFV SWISSPROT:CHLB_PINTH ID CHLB_PINTH STANDARD; PRT; 510 AA. AC Q00864; DT 01-APR-1993 (REL. 25, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS PINUS THUNBERGII (GREEN PINE) (JAPANESE BLACK PINE). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92212283. RA TSUDZUKI J., NAKASHIMA K., TSUDZUKI T., HIRATSUKA J., SHIBATA M., RA WAKASUGI T., SUGIURA M.; RL MOL. GEN. GENET. 232:206-214(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 95024047. RA WAKASUGI T., TSUDZUKI J., ITO S., NAKASHIMA K., TSUDZUKI T., RA SUGIURA M.; RL PROC. NATL. ACAD. SCI. U.S.A. 91:9794-9798(1994). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; D11467; G344008; -. DR EMBL; D17510; G1262591; -. DR PIR; S29324; S29324. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 510 AA; 57741 MW; 3FB5A6C6 CRC32; >CHLB_PINTH MKLAHWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERNFTPATASIV DRHVLARGSRKRVVDHIIRKDKEEGPDLIILTPTCTSSILQEDLKNFVDRASIISDCNVI FADVDHYQVNEIQAADRTLEQVVRYYLEKSHTLDQFVTDAPSVNIIGILTLGFHNRHDCR ELRRLLKDLDIRINQIIPEGGSVEDPKNLPKARFNLIPYREVGLMTAMYLNKEFGMPYVS TTPMGAVDMAECIRQIKKSLETLAAPILSSKRVDYESYIDGQTRFVSQAAWFSRSIDCQN FTGKETVVFGDATHAASITKILAREMGIRVSCTGTYCKHDAEWFKEQIKDFCDEIIITDD HAEVGDIISRVEPSAIFGTQMERHIGKRLEIPCGVISAPAHIQNFSLGYRPFLGYEGTNQ IADLVYNSFALGMEDHLLDIFCGHDTKEIMTKSLSTDISPIWDPESRQELGKIPRFVRDE VKRNTEKFARRKGILNVTVEVMHAAKEALS SWISSPROT:CHLB_PICMA ID CHLB_PICMA STANDARD; PRT; 104 AA. AC P37853; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS PICEA MARIANA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25773; G495060; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 104 104 SQ SEQUENCE 104 AA; 11890 MW; BACC9F00 CRC32; >CHLB_PICMA RRLLKDLDIRINQIIPEGGSVEDSKNLPKARFNLIPYREVGLMTAMYLNKEFGMPYVSTT PMGAVDMAECIRQIKKYIDTLAAPILSSKRVDYESYIDGQTRFV SWISSPROT:CHLB_OSMCL ID CHLB_OSMCL STANDARD; PRT; 103 AA. AC P37851; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS OSMUNDA CLAYTONIANA (FERN). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; FILICOPHYTA; FILICALES. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25771; G495058; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11661 MW; A43CD11E CRC32; >CHLB_OSMCL KRLPGESGVSVNQVIPEGASLKYLKDLPRAWFNAVPYREVGLMTATFSEKEYGMPYISIT PMGISNTADFIEQIGKLVNVWASVLSERKLNYRLYVENQTKFV SWISSPROT:CHLB_NEPEX ID CHLB_NEPEX STANDARD; PRT; 103 AA. AC P37850; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS NEPHROLEPIS EXALTATA (FERN). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; FILICOPHYTA; FILICALES. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25770; G495055; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11787 MW; 9DE0A846 CRC32; >CHLB_NEPEX KRLLGESGIAVNQVIPEGGYLNYLKDLPRAWFNIVPYREVGLMTAIFSEKEYGMPYISIT PMGISNTANFIAQIEKLVNMWASALSEKRLNYKFYVDNQTKFV SWISSPROT:CHLB_METGY ID CHLB_METGY STANDARD; PRT; 103 AA. AC P37849; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS METASEQUOIA GLYPTOSTROBOIDES. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25769; G495052; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11893 MW; C6AD3835 CRC32; >CHLB_METGY RRLLRDLNIEINQIIPEGGSVKDLKNLPKAWFNLIPYREVGLMTAMYLNKEYGMPYISTA PMGAVDMAEWIRQIQKNVNTLALSLSSKRVDYEPYIDGQTRFV SWISSPROT:CHLB_MARPO ID CHLB_MARPO STANDARD; PRT; 513 AA. AC P26238; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS MARCHANTIA POLYMORPHA (LIVERWORT). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; HEPATICOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA OHYAMA K.; RL SUBMITTED (OCT-1986) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP COMPLETE GENOME. RA OHYAMA K., FUKUZAWA H., KOHCHI T., SHIRAI H., SANO T., SANO S., RA UMESONO K., SHIKI Y., TAKEUCHI M., CHANG Z., AOTA S., INOKUCHI H., RA OZEKI H.; RL NATURE 322:572-574(1986). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE; 89068686. RA UMESONO K., INOKUCHI H., SHIKI Y., TAKEUCHI M., CHANG Z., FUKUZAWA H., RA KOHCHI T., SHIRAI H., OHYAMA K., OZEKI H.; RL J. MOL. BIOL. 203:299-331(1988). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; X04465; G11661; -. DR PIR; A05029; A05029. DR PIR; S01586; S01586. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 513 AA; 58327 MW; 8EF1B072 CRC32; >CHLB_MARPO MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIV DRHVLARGSQEKVVDNITKKDKQEHPDLIVLTPTCTSSILQEDLQNFVNRASMSSDSDVI LADVNHYRVNELQAADRTLEQVVRYYLEKAHRQEKLNLSLTDKPSANIIGIFTLGFHNQH DCRELKRLLQDLGIMINQIIPEGGFVENLHELPKAWFNLVPYREVGLMTALYLEKEFGMP YISTTPMGIVDIANCIRQIQKQVNIWSPILLGKKFDFEPYIDEQTRFISQAAWFSRSIDC QNLTGKKAVVFGDATHAASITKILACEMGIRVSCTGTYCKHDEEWFREQVQNFCDEILIT DDHTEVGDMIARIEPSAIFGTQMERHIGKRLDIPCGVISSPVHIQNFPLGYRPFLGYEGT NQIADLVYNSFTLGMEDHLLEIFGGHDTKEVITKSLSTDTDLTWNSESQLELNKIPGFVR GKIKRNTEKFARQNNITKITVEVMYAAKEDLSA SWISSPROT:CHLB_LYCCO ID CHLB_LYCCO STANDARD; PRT; 103 AA. AC P37848; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS LYCOPODIUM COMPLANATUM. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; LYCOPODIOPHYTA; LYCOPODIOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25768; G495050; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11926 MW; 10D55773 CRC32; >CHLB_LYCCO KRLLQNLGIEINQVIPEGGFVEDLQNLPKAWFNFVPYREIGLMTAVYLEKEFGMPYVSIT PMGIVDTAECIRQIQKHINELAVVSLEETVDYEPYIYQQTKFV SWISSPROT:CHLB_LYCAN ID CHLB_LYCAN STANDARD; PRT; 103 AA. AC P37847; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS LYCOPODIUM ANNOTINUM. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; LYCOPODIOPHYTA; LYCOPODIOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25767; G495048; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11940 MW; 57A99199 CRC32; >CHLB_LYCAN KRLLQNLGIEINQVIPEGGFIEDLQNLPKAWFNFVPYREIGLMTAVYLEKEFGMPYVSIT PMGIVDTAECIRQIQKHINELAVVSLEETVDYEPYIYQQTKFV SWISSPROT:CHLB_GINBI ID CHLB_GINBI STANDARD; PRT; 513 AA. AC P36208; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS GINKGO BILOBA (GINKGO). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; GYMNOSPERMAE; GINKGOALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95094313. RA RICHARD M., TREMBLAY C., BELLEMARE G.; RL CURR. GENET. 26:159-165(1994). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; U01531; G476119; -. DR PIR; S45486; S45486. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 513 AA; 58138 MW; 969B6565 CRC32; >CHLB_GINBI MKLAHWMYAGPAHIGTLRVASSSKNVHAIMHAPLGHHYFNVMRSMLERERDFTPATASTV DRHVLARGSQEKVVDNVLRKDKEERPDLIILTPTCTSSILQEDLQNFADRASIISDSNVI FADVDHYRVNELQAADRTLEQVVRYYLDRSHRQETLDQSVTDAPSANLIGIFTLGFHNQH DCRELRRLLRDLDIEMNQVIPEGGSVEDLKNLPKAWLNLIPYREVGLMTAMYFEKEFGMP YISTIPMGAVDMAECIRQIQRYVNTLAHISSSKEVDYEPYIDGQTRFVSQAAWFSRSIDC QNLTGKETVVFGDATHAASITKIPAREMGIRVSYTGTYCENDAEWFKEQIQGFCDEILIT DDHIKVGDMIARAEPSALFGTQMERHIGKRLDIPRGVISSPVHIQNFSLGYRPFLGYEGT NQIADPVYNTFALGMEDHLLDLFGGHDTKEIMTKSSSTDIGPIWNSESRLELSKIPRFAR SKVERNTEQFARQKGIVNITVEVMYAAKEVLNA SWISSPROT:CHLB_EQUAR ID CHLB_EQUAR STANDARD; PRT; 103 AA. AC P37845; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS EQUISETUM ARVENSE (FIELD HORSETAIL) (COMMON HORSETAIL). OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; EQUISETOPHYTA; SPHENOPSIDA; OC EQUISETALES; EQUISETACEAE. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25766; G495023; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11923 MW; FF279F0C CRC32; >CHLB_EQUAR KRLLEDLGIKINEIIPEGASVKNLINLPKAWFNIVPYREVGLMTASFLQKDFGMPYILTT PMGIIDTADFIRQVQKNVNKLAPFFLNKTFDYESYIDYQTKFV SWISSPROT:CHLB_EPHAL ID CHLB_EPHAL STANDARD; PRT; 103 AA. AC P37846; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS EPHEDRA ALTISSIMA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; GNETICAE. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25765; G495026; -. DR HSSP; P11347; 1MIO. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11886 MW; 337ACA02 CRC32; >CHLB_EPHAL KRLFQDLNIQINQVIPEGGSVEDLQNLPKAWLNLVPYREIGLMTAFFLKKEFGMPYLSIT PMGVIDNAECIRRIEKSVNPFASIFGEKGVNYESYIDRQTRFI SWISSPROT:CHLB_CYAPA ID CHLB_CYAPA STANDARD; PRT; 440 AA. AC P48099; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS CYANOPHORA PARADOXA. OG CYANELLE. OC EUKARYOTA; PLANTA; PHYCOPHYTA; GLAUCOPHYTA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LB555 / PRINGSHEIM; RA STIREWALT V.L., MICHALOWSKI C.B., LUFFELHARDT W., BOHNERT H.J., RA BRYANT D.A.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; U30821; G1016093; -. KW CYANELLE; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 440 AA; 50284 MW; 9E06A9F7 CRC32; >CHLB_CYAPA MKLAYWMYTGPAHIGTLRIASSFKNVHAIMHAPLGDDYFNVMRSMLERERNYTPVTTSVV DRNVLARGSQEKVIDNILRKDKEEQPDLIVLTPTCTSSILQEDLQNFVEQASLNSMADVL LADVNHYRINELQACDKTLEQIVRFYIEKNRASLTLEKVKTLLPSVNLIGISSLGFHNNH DTRELKKLFELYEIILNCSLPQGTTVKTLINLPKAWLNILPYRELGLLTSKYLNKEFGLL SLVILPMGNINLNRFLKKLLFSLKLENNTITKVINIKLLKLLNLNWIKKEAIKSKLKRKK AIIFGSSNHVATLTKLLSKEIGLEIILCGTYCKSESKWFSEQVQNYCNKILITEDHTMIS NEISKLKPDVIFGTQMERHIGKRLGIPCGVISSPIHIQNFPLSYKPMVGYEGVKTIMDLL FNSLNLKDRKNSFTLFNEII SWISSPROT:CHLB_CHLRE ID CHLB_CHLRE STANDARD; PRT; 688 AA. AC P36437; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS CHLAMYDOMONAS REINHARDTII. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=137C; RX MEDLINE; 94033309. RA LIU X.-Q., XU H., HUANG C.; RL PLANT MOL. BIOL. 23:297-308(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=21GR; RX MEDLINE; 94138245. RA LI J., GOLDSCHMIDT-CLERMONT M., TIMKO M.; RL PLANT CELL 5:1817-1829(1993). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L13782; G406069; -. DR EMBL; U02526; G463361; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT CONFLICT 44 44 T -> S (IN REF. 2). FT CONFLICT 210 210 D -> N (IN REF. 2). FT CONFLICT 532 532 A -> R (IN REF. 2). FT CONFLICT 616 616 V -> G (IN REF. 2). FT CONFLICT 623 626 FKCS -> SNV (IN REF. 2). FT CONFLICT 628 628 F -> S (IN REF. 2). SQ SEQUENCE 688 AA; 76822 MW; 13E493EA CRC32; >CHLB_CHLRE MKLAYWMYAGPAHIGVLRVSSSFKNVHAIMHAPLGDDYFNVMRTMLERERDFTPVTASIV DRHVLARGSQEKVVENITRKNKEETPDLILLTPTCTSSILQEDLHNFVESALAKPVQIDE HADHKVTQQSALSSVSPLLPLEENTLIVSELDKKLSPSSKLHINMPNICIPEGEGEGEQT KNSIFVKSATLTNLSEEELLNQEHHTKTRDHSDVILADVNHYRVNELQAADRTLEQIVRY YISQAQKQNCLNITKTAKPSVNIIGIFTLGFHNQHDCRELKRLFNDLGIQINEIIPEGGN VHNLKKLPQAWFNFVPYREIGLMTAMYLKSEFNMPYVAITPMGLIDTAACIRSICKIITT QLLNQTATVQEPSKFIYPKATSLEQTNILETSQKETILKDNPDSGNTLSTTVEEIETLFN KYIDQQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHSAAMTKLLAREMGIKVSCAGTY CKHDADWFREQVSGFCDQVLITDDHTQVGDMIAQLEPAAIFGTQMERHVGKALDIPCGVI SAPVHIQNFPLGYRPFLGYEGTNQIADLVYNSFNLGMEDHLLQIFGGHDSENNSSIATHL NTNNAINLAPGYLPEVEGSSRTFKCSVFTISSEKKAIVWSPEGLAELNKVPGFVRGKVKR NTEKYALQKNCSMITVEVMYAAKEALSA SWISSPROT:CHLB_CHLPT ID CHLB_CHLPT STANDARD; PRT; 444 AA. AC P37824; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS CHLAMYDOMONAS PITSCHMANNII. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94033309. RA LIU X.-Q., XU H., HUANG C.; RL PLANT MOL. BIOL. 23:297-308(1993). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 444 444 SQ SEQUENCE 444 AA; 50058 MW; B9C005C5 CRC32; >CHLB_CHLPT MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTTSIV DRHVLARGSQEKVVENITRKDNEEAPDLITLTPTCTSSILQEDLQIFVNRASISESNNGH SGIDKATSDVILADVNHYRVNELQAADRTLEQIVRFYLEKEKKLNTNTIPTKTKKPSANI IGIFTLGFHNQHDCRELKRLLNNLGIEVNEIIPEGGSVTNLKNLPHAWFNLVPYREIGLM RAVYLEKEFNMPYVAISPLGIIDTAVCIREIEKILNNLSLNGYQSSLPEGHKLTNEELNG LSQKNNEPSLPEEHRQLDGALDSKSQKTYNFENKYIKQQTRFISQAAWFSRSIDCLNLTA KKAVVFGDATHAAGITKILAREMGIKVVCSGTYCKHDADWFREQVVGFCDQILVTDDHTQ VGDMIAKLEPSAIFGTQMERHIGR SWISSPROT:CHLB_CHLMO ID CHLB_CHLMO STANDARD; PRT; 563 AA. AC P17652; DT 01-AUG-1990 (REL. 15, CREATED) DT 01-AUG-1990 (REL. 15, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT). GN CHLB. OS CHLAMYDOMONAS MOEWUSII. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=UTEX 97; RX MEDLINE; 90272427. RA RICHARD M., BELLEMARE G.; RL NUCLEIC ACIDS RES. 18:3061-3061(1990). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; X51398; G11368; -. DR PIR; S10176; S10176. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 563 AA; 63610 MW; 9277FDA8 CRC32; >CHLB_CHLMO MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTTSIV DRHVLARGSQEKVVENITRKDNEESPDLIILTPTCTSSILQEDLQNFVNRASMSENSTSD VLLADVNHYRVNELQAADRTLEQIVRFYLEKEKSTLFRQGVSSVDDNNKTLTNNFLSIKT EKPSANIIGIFTLGFHNQHDCRELKRLLNNLGIEINEVIPEGGSVKNLKNLPKAWFNIIP YREVGLMSAIYLEKEFNMPYVAVSPIGIIDTAVCIREIERILNKIYFESLEGNVNTQSVL TTNPYFNSHINSTNSETRDHNVKPFDFEFYIENQTRFISQAAWFSRSIDCQNLTGKKAVV FGDATHAAGITKILAREMGIKVVCSGTYCKHDADWFREQVFGFCDQILITDDHTQVGDMI AKLEPSAIFGTQMERHIGKRLDIPCGVISAPVHIQNFPLSYRPFLGYEGTNQIADLVYNS FSLGMEDHLLEIFSGHDTKEPITKSLSTENELNWDAEALKELSNVPGFVRGKVKRNTEKY ARQNAIPSITLDVLFAAKEALSA SWISSPROT:CHLB_CHLHU ID CHLB_CHLHU STANDARD; PRT; 431 AA. AC P37823; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS CHLAMYDOMONAS HUMICOLA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94033309. RA LIU X.-Q., XU H., HUANG C.; RL PLANT MOL. BIOL. 23:297-308(1993). CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 431 431 SQ SEQUENCE 431 AA; 48004 MW; E0E1735B CRC32; >CHLB_CHLHU MKLAESMYAGPAHIGTLRVASSFRNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIV DRHVLARGSQEKVVENIQRKDKEESPDLILLTPTCTSSILQEDLQNFVNRASETSTSDVL LADVNHYRVNELQAADRTLEQIVRFYIEKTRAKDPGSPDPGGAGRRQASSSTESGTEENL KGACGGEKTKKPSANILGMFTLGFHNQHDCRELKRLLAELDIEVNEVIPEGGLVSNLKNL PKAWFNIVPYREVGLMTAVYLEKEFGMPYTSTTPMGIIQTSAFIREMALMCHEVYNNSST KCSQTDFESCLISNTKKVPKTYINKQTHFVSQAGWFARSIDCQNLTGQKTVVFGDATHAA SMTKILVREMGIHVVCAGTYCKHDADWFREQVSGFCDQVLITDDHSQIGDIISQIEPAAI FGTQMERHIGK SWISSPROT:CHLB_BAZTR ID CHLB_BAZTR STANDARD; PRT; 103 AA. AC P37844; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS BAZZANIA TRILOBATA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; HEPATICOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25764; G495015; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 12061 MW; 97BF491B CRC32; >CHLB_BAZTR KRLLKDLSIEINQVIPEGGSVENLRQLPKAWFNLVPYREVGLMTAKYLEKEFGMSYISIT PMGVVDIANCIRQMEERINIMSPILLNRRVNYEPYINEQTRFI SWISSPROT:CHLB_ARAHE ID CHLB_ARAHE STANDARD; PRT; 103 AA. AC P37843; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE CHLB SUBUNIT (EC 1.3.1.33) (NADPH- DE PROTOCHLOROPHYLLIDE OXIDOREDUCTASE CHLB SUBUNIT) (FRAGMENT). GN CHLB. OS ARAUCARIA HETEROPHYLLA. OG CHLOROPLAST. OC EUKARYOTA; PLANTA; EMBRYOPHYTA; CONIFEROPHYCEAE. RN [1] RP SEQUENCE FROM N.A. RA BOIVIN R., RICHARD M., BOUSQUET J., BELLEMARE G.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INVOLVED IN THE LIGHT-INDEPENDENT ACCUMULATION OF CC CHLOROPHYLL, PROBABLY AT THE STEP OF REDUCTION OF PROTO- CC CHLOROPHYLLIDE TO CHLOROPHYLLIDE (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: LIGHT-INDEPENDENT CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO R.CAPSULATUS BCHB AND OTHER PLANTS PLASTID CHLB. DR EMBL; L25763; G495009; -. KW CHLOROPLAST; PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 1 1 FT NON_TER 103 103 SQ SEQUENCE 103 AA; 11782 MW; B5318A5B CRC32; >CHLB_ARAHE RRLLRDLDIEINQIIPEGGSVEDLKDLPKAWFNLIPYREVGLMTAIYLNKEFGMPYISTA PMGAVDIAEWIRQIHKNVNTLAPSSSSKKVDYEPYIDGQTRFV SWISSPROT:BCHN_RHOCA ID BCHN_RHOCA STANDARD; PRT; 424 AA. AC P26164; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE 46 KD CHAIN (EC 1.3.1.33). GN BCHN. OS RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB1003; RX MEDLINE; 93224465. RA BURKE D.H., ALBERTI M., HEARST J.E.; RL J. BACTERIOL. 175:2414-2422(1993). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: BACTERIOCHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO CHLN FROM SOME PLANTS CHLOROPLAST. DR EMBL; Z11165; G46109; -. DR PIR; S17810; S17810. DR PIR; B49851; B49851. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 424 AA; 45829 MW; 355C62AB CRC32; >BCHN_RHOCA MSLDSPTFGCTDSPVRRERGQKAVFCGLTSIVWLHRKMQDAFFLVVGSRTCAHLLQAAAG VMIFAEPRFGTAVLEEQDLAGLADAHKELDREVAKLLERRPDIRQLFLVGSCPSEVLKLD LDRAAERLSGLHAPHVRVYSYTGSGLDTTFTQGEDTCLAAMVPTLDTTEAAELIVVGALP DVVEDQCLSLLTQLGVGPVRMLPARRSDIEPAVGPNTRFILAQPFLGETTGALERRGAKR IAAPFPFGEEGTTLWLKAVADAYGVSAEKFEAVTAAPRARAKKAIAAHLETLTGKSLFMF PDSQLEIPLARFLARECGMKTTEIATPFLHKAIMAPDLALLPSNTALTEGQDLEAQLDRH EAINPDLTVCGLGLANPLEAKGHATKWAIELVFTPVHFYEQAGDLAGLFSRPLRRRALLN GGAA SWISSPROT:BCHB_RHOCA ID BCHB_RHOCA STANDARD; PRT; 525 AA. AC P26163; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE REDUCTASE 57 KD CHAIN (EC 1.3.1.33). GN BCHB OR BCHK. OS RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB1003; RX MEDLINE; 93224465. RA BURKE D.H., ALBERTI M., HEARST J.E.; RL J. BACTERIOL. 175:2414-2422(1993). CC -!- FUNCTION: REQUIRED FOR PROTOCHLOROPHYLLIDE REDUCTION IN THE DARK. CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. CC -!- PATHWAY: BACTERIOCHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO CHLB FROM SOME PLANTS CHLOROPLAST AND TO BCHZ. DR EMBL; Z11165; G46108; -. DR PIR; S17809; S17809. DR PIR; C49851; C49851. KW PHOTOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 525 AA; 57191 MW; 84BA6766 CRC32; >BCHB_RHOCA MKLTLWTYEGPPHVGAMRVATAMKDLQLVLHGPQGDTYADLLFTMIERRNARPPVSFSTF EASHMGTDTAILLKDALAAAHARYKPQAMAVALTCTAELLQDDPNGISRALNLPVPVVPL ELPSYSRKENYGADETFRALVRALAVPMERTPEVTCNLLGATALGFRHRDDVAEVTKLLA TMGIKVNVCAPLGASPDDLRKLGQAHFNVLMYPETGESAARHLERACKQPFTKIVPIGVG ATRDFLAEVSKITGLPVVTDESTLRQPWWSASVDSTYLTGKRVFIFGDGTHVIAAARIAA KEVGFEVVGMGCYNREMARPLRTAAAEYGLEALITDDYLEVEKAIEAAAPELILGTQMER NIAKKLGLPCAVISAPVHVQDFPARYAPQMGFEGANVLFDTWVHPLVMGLEEHLLTMFRE DFEFHDAAGASHHGGKAVAREESPVAPADLAPAATSDTPAAPSPVVVTQASGEIRWMPEA ERELRKIPFFVRGKAKRNTELYAAHKGVCDITVETLYEAKAHYAR TREMBL:Q59987 ID Q59987 PRELIMINARY; PRT; 318 AA. AC Q59987; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE PROTOCHLOROPHYLLIDE OXIDO-REDUCTASE (EC 1.3.1.33) DE (PROTOCHLOROPHYLLIDE REDUCTASE) DE (NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). GN NADPH. OS SYNECHOCYSTIS SP. OC PROKARYOTA; BACTERIA; GRACILICUTES; OXYPHOTOBACTERIA; CYANOBACTERIA; OC CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PCC 6803; RX MEDLINE; 95249551. RA SUZUKI J.Y., BAUER C.E.; RL PROC. NATL. ACAD. SCI. U.S.A. 92:3749-3753(1995). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. DR EMBL; L37783; G829038; -. KW OXIDOREDUCTASE; CHLOROPHYLL. SQ SEQUENCE 318 AA; 35661 MW; FA22715B CRC32; >Q59987 MKPTVIITGASSGVGLYGRKALIDKGWHVIMACRNLDKTQKVADELGFPKDSYTIIKLDL GYLDSVRRFVAQFRELGRPLKALVCNAAVYFPLLDEPLWSADDYELSVATNHLGHFLLCN LLLEDLKACPDADKRLIILGTVTANSKELGGKIPIPAPPDLGNFEGFEAGFKKPIAMINN KKFKSGKAYKDSKLCNMLTTRELHRRFHQETGIVFNSLYPGCVADTPLFRNHYSLFRTIF PWFQKNVTKGYVSQELAGERVAMVVADDKFKDSGVHWSWGNRQQAGREAFVQELSEQGSD AQKAQRMWDLSEKLVGLV TREMBL:Q42537 ID Q42537 PRELIMINARY; PRT; 401 AA. AC Q42537; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE B PRECURSOR (EC 1.3.1.33) DE (PROTOCHLOROPHYLLIDE REDUCTASE) DE (NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). GN PORB. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=WHOLE PLANT; RX MEDLINE; 95388766. RA ARMSTRONG G.A., RUNGE S., FRICK G., SPERLING U., APEL K.; RL PLANT PHYSIOL. 108:1505-1517(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=WHOLE PLANT; RX MEDLINE; 91329695. RA BENLI M., SCHULZ R., APEL K.; RL PLANT MOL. BIOL. 16:615-625(1991). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. DR EMBL; U29785; G968977; -. KW TRANSIT PEPTIDE; OXIDOREDUCTASE. FT TRANSIT 1 66 POTENTIAL. FT CHAIN 67 401 NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE FT B. SQ SEQUENCE 401 AA; 43359 MW; C9100CB0 CRC32; >Q42537 MALQAASLVSSAFSVRKDAKLNASSSSFKDSSLFGASITDQIKSEHGSSSLRFKREQSLR NLAIRAQTAATSSPTVTKSVDGKKTLRKGNVVVTGASSGLGLATAKALAETGKWNVIMAC RDFLKAERAAKSVGMPKDSYTVMHLDLASLDSVRQFVDNFRRTETPLDVLVCNAAVYFPT AKEPTYSAEGFELSVATNHLGHFLLARLLLDDLKKSDYPSKRLIIVGSITGNTNTLAGNV PPKANLGDLRGLAGGLNGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRFHEETGV TFASLYPGCIASTGLFREHIPLFRALFPPFQKYITKGYVSETESGKRLAQVVSDPSLTKS GVYWSWNNASASFENQLSEEASDVEKARKVWEISEKLVGLA TREMBL:Q42536 ID Q42536 PRELIMINARY; PRT; 405 AA. AC Q42536; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE A PRECURSOR (EC 1.3.1.33) DE (PROTOCHLOROPHYLLIDE REDUCTASE) DE (NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE). GN PORA. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=WHOLE PLANT; RX MEDLINE; 95388766. RA ARMSTRONG G.A., RUNGE S., FRICK G., SPERLING U., APEL K.; RL PLANT PHYSIOL. 108:1505-1517(1995). CC -!- CATALYTIC ACTIVITY: CHLOROPHYLLIDE A + NADP(+) = CC PROTOCHLOROPHYLLIDE + NADPH. DR EMBL; U29699; G968975; -. KW TRANSIT PEPTIDE; OXIDOREDUCTASE. FT TRANSIT 1 69 POTENTIAL. FT CHAIN 70 405 NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE FT A. SQ SEQUENCE 405 AA; 43877 MW; 0D6CF912 CRC32; >Q42536 MALQAASLVSSAFSVRKDGKLNASASSSFKESSLFGISLSEQSKADFVSSSLRCKREQSL RNNKAIIRAQAIATSTPSVTKSSLDRKKTLRKGNVVVTGASSGLGLATAKALAETGKWHV IMACRDFLKAERAAQSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRAEMPLDVLVCNAAV YQPTANQPTFTAEGFELSVGINHLGHFLLSRLLIDDLKNSDYPSKRLIIVGSITGNTNTL AGNVPPKANLGDLRGLAGGLNGLNSSAMIDGGDFVGAKAYKDSKVCNMLTMQEFHRRFHE DTGITFASLYPGCIATTGLFREHIPLFRTLFPPFQKYITKGYVSESEAGKRLAQVVADPS LTKSGVYWSWNKTSASFENQLSQEASDVEKARRVWEVSEKLVGLA TREMBL:Q41249 ID Q41249 PRELIMINARY; PRT; 398 AA. AC Q41249; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE. OS CUCUMIS SATIVUS (CUCUMBER). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC VIOLALES; CUCURBITACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95275277. RA KURODA H., MASUDA T., OHTA H., SHIOI Y., TAKAMIYA K.; RL BIOCHEM. BIOPHYS. RES. COMMUN. 210:310-316(1995). DR EMBL; S78381; G998907; -. SQ SEQUENCE 398 AA; 43074 MW; 1482B77F CRC32; >Q41249 MALQAASLVSPALSIPKEGKSSVCLKDSSLFGISFSDHLKSEFSSSTLRCKRELNQQIGA IRAQTTATESPAVNKATPDGKKTLRKGSVVITGASSGLGLATAKALAETGKWHVIMACRD FLKAERAAKSAGITKENYTVMHLDLASLDSVRQFVDNFRQSGRPLDVLVCNAAVYLPTAK EPTFTAEGFELSVGTNHLGHFLLSRLLLEDLNKSSYPSKRLIIVGSITGNTNTLAGNVPP KANLGDLRGLAGGLNGLKSSMIDGGEFDGAKAYKDSKVCNMLTMQEFHKRYHEETGITFA SLYPGCIATTGLFREHIPLFRILFPPFQKFITQGYVSEDEAGKRLAQVVSEPSLTKSGVY WSWNKNSASFENQLSQEASDAEKARKVWELSEKLVGLA TREMBL:Q41203 ID Q41203 PRELIMINARY; PRT; 199 AA. AC Q41203; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NADPH-PROTOCHLOROPHYLLIDE-OXIDOREDUCTASE (FRAGMENT). OS PINUS MUGO. OC EUKARYOTA; PLANTAE; EMBRYOBIONTA; PINOPHYTA; PINICAE; PINATAE; OC PINACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93326951. RA FORREITER C., APEL K.; RL PLANTA 190:536-545(1993). DR EMBL; S63825; E98368; -. FT NON_TER 1 1 FT NON_TER 199 199 SQ SEQUENCE 199 AA; 21955 MW; 01C24EFF CRC32; >Q41203 FLLSRLLLEDLKKSDFKSKRVIIVGSITGNTNTLAGNIPPKANLGDLRGFSARLNGVNSS PMIDGGEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFASLYPGCIATTGLFREHIPP FKLSFPPSQKYITKGFVSEEEAGKRLAQVVSDPSLTKSGGYWSWNNDSSSFENQLSEEAS DPRKARKVWGISEKLVGLA TREMBL:Q41202 ID Q41202 PRELIMINARY; PRT; 400 AA. AC Q41202; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE NADPH-PROTOCHLOROPHYLLIDE-OXIDOREDUCTASE (FRAGMENT). OS PINUS MUGO. OC EUKARYOTA; PLANTAE; EMBRYOBIONTA; PINOPHYTA; PINICAE; PINATAE; OC PINACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93326951. RA FORREITER C., APEL K.; RL PLANTA 190:536-545(1993). DR EMBL; S63824; E98367; -. FT NON_TER 400 400 SQ SEQUENCE 400 AA; 43472 MW; 21058485 CRC32; >Q41202 MGTLLQTHIGSVAFALQKEGGHSASAKDSAFLGVSLVEHGKKEFSFPVIRAKKVTSRNTN VPRIRAQTVAAPVETKDAPASKKTDRKGNVIITGASSGLGLATAKALGESGKWHIIMACR DFLKAERMARSVGIPKENYSVMHLDLASLESVRQFADNFRRSGRPLDVLVCNAAIYLPTA KLPTYTAEGFELSVGTNHLGHFLLSRLLLEDLKTSDFNSKRVIIVGSITGNTNTLAGNVP PKANLGDLRGLAGGLNGVNISPMIDGGEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGIT FASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGFVSEEEAGKRLAQVVSNPSLTKSG VYWSWNNNSGSFENQLSEEASDPEKAKKLWEISEKLVGLA