Version 2.0

Database Object View

SWISSPROT:HEM4_YEAST

ID HEM4_YEAST STANDARD; PRT; 275 AA. AC P06174; DT 01-JAN-1988 (REL. 06, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)) DE (UROIIIS). GN HEM4 OR ORF1 OR YOR278W OR O5463. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 28583 / FL100; RX MEDLINE; 88194672. RA LANGGUT W., ENTRUP R., SCHWEIZER E.; RL CURR. GENET. 11:177-184(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RA CHERET G., BERNARDI A., SOR F.J.; RL YEAST 12:1059-1064(1996). RN [3] RP CHARACTERIZATION. RX MEDLINE; 95321013. RA AMILLET J.M., LABBE-BOIS R.; RL YEAST 11:419-424(1995). CC -!- FUNCTION: INVOLVED IN MITOCHONDRIAL IMPORT OF CYTOPLASMICALLY CC SYNTHESIZED PRECURSOR PROTEINS. CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO BE INVOLVED IN CC MITOCHONDRIAL IMPORT. DR EMBL; X04694; G4085; -. DR EMBL; X89633; E189403; -. DR PIR; S05883; RGBY7K. DR SGD; L0002903; HEM4. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE. FT CONFLICT 231 275 HLRVASIGPTTKKYLDDNDVTSDVVSPKPDPKSLLDAIELY FT QRHK -> IYGLRHRTYH (IN REF. 1). SQ SEQUENCE 275 AA; 30911 MW; 66F4292D CRC32; >HEM4_YEAST MSSRKKVRVLLLKNKTVPIDKYELECRSKAFEPIFVPLIKHTHVIQDFRNVLNTIPNYLN TINYIIITSQRTVESLNEAIIPTLTSEQKAALLSKTVYTVGPATANFIRRSGFINVKGGE DAGNGSILADIIIDDLSTDIKACPPSELLFLVGEIRRDIIPKKLHSKGIKVREVVTYKTE ELSDGFKRFIHAMKECDEDEVFSDWVVVFSPQGTKEITQYLGDSNRLPGSHLRVASIGPT TKKYLDDNDVTSDVVSPKPDPKSLLDAIELYQRHK


SWISSPROT:HEM4_SYNP7

ID HEM4_SYNP7 STANDARD; PRT; 264 AA. AC P42452; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)). GN HEMD. 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. RX MEDLINE; 94169298. RA JONES M.C., JENKINS J.M., SMITH A.G., HOWE C.J.; RL PLANT MOL. BIOL. 24:435-448(1994). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS. DR EMBL; X70966; G471285; -. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT ACT_SITE 146 146 POTENTIAL. SQ SEQUENCE 264 AA; 28196 MW; D85E124A CRC32; >HEM4_SYNP7 MAEQPLIGKTILTTRAAGQSSPFAAQLRAAGAAVIEMPTLEIGPPSSWLPLDEAIAAIAD FDWLILASANAVEAVQQRLAAQQKSWSDVPCAIAVVGQKTAQVLAAQGGKADYIPPEFIA ESLVEHFPQPVAGQRLLFPRVETGGREQITQALQSQGAIVVEVPAYESRCPSQIPDDALI ALRQAHLNLISFTSSKTVRNFCQLMASNLGVDWSARISGVAIASIGPQTSITCQELLGRV EVEAQEYTLDGLLLAIEQWARQTT


SWISSPROT:HEM4_PSEAE

ID HEM4_PSEAE STANDARD; PRT; 251 AA. AC P48246; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)). GN HEMD. OS PSEUDOMONAS AERUGINOSA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94211207. RA MOHR C.D., SONSTEBY S.K., DERETIC V.; RL MOL. GEN. GENET. 242:177-184(1994). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS. DR EMBL; M74844; G496215; -. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT ACT_SITE 142 142 POTENTIAL. SQ SEQUENCE 251 AA; 27105 MW; B842496C CRC32; >HEM4_PSEAE MSGWRLLLTRPDEECAALAASLGEAGVHSSSLPLLAIDPLEETPEQRTLMLDLDRYCAVV VVSKPAARLGLERLDRYWPQPPQQTWCSVGAATAAILEAYGLDVTYPEQGDDSEALLALP AFQDSLRVHDPKVLIMRGEGGREFLAERLRGQGVQVDYLPLYRRRAPDYPAGELLARVRA ERLNGLVVSSGQGLPKSVSVGGSDWPEIGRLPLFVPSPRVAEMARELGAQRVIDCRGASA PALLAALTSAA


SWISSPROT:HEM4_MOUSE

ID HEM4_MOUSE STANDARD; PRT; 265 AA. AC P51163; 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 UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)) DE (UROIIIS). GN UROS. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B6/CBAF1J; TISSUE=LIVER; RX MEDLINE; 95331792. RA XU W., KOZAK C.A., DESNICK R.J.; RL GENOMICS 26:556-562(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 95178849. RA BENSIDHOUM M., GED C.M., POIRIER C., GUENET J.L., DE VERNEUIL H.; RL MAMM. GENOME 5:728-730(1994). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). DR EMBL; U18867; G953228; -. DR EMBL; U16216; G1041679; -. DR EMBL; U04439; G506638; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE. SQ SEQUENCE 265 AA; 28504 MW; B888D2C2 CRC32; >HEM4_MOUSE MKVLLLKDAKEDDSGLDPYIQELRLCGLEATLIPVLSFEFMSLPSLSEKLSHPEGFGGLI FTSPRAVEAVKLCLEKDNKTEAWEKSLKDRWNAKSVYVVGSATASLVNKIGLDAEGAGSG NAEKLAEYICSKPSSELPLLFPCGTIKGDTLPKMLKDKGIPMESMHVYQTVPHPGIQGSL KSYYEDQGIPASITFFSPSGLKYSLEYIQALSGSSFDQIKFIAIGPSTTRAMAAKGLPVS CTAESPTPQALAAGIRNVLKPNHCC


SWISSPROT:HEM4_HUMAN

ID HEM4_HUMAN STANDARD; PRT; 265 AA. AC P10746; DT 01-JUL-1989 (REL. 11, CREATED) DT 01-JUL-1989 (REL. 11, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)) DE (UROIIIS). GN UROS. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE; 89017136. RA TSAI S.-F., BISHOP D.F., DESNICK R.J.; RL PROC. NATL. ACAD. SCI. U.S.A. 85:7049-7053(1988). RN [2] RP REVIEW ON VARIANTS. RX MEDLINE; 96271980. RA XU W., ASTRIN K.H., DESNICK R.J.; RL HUM. MUTAT. 7:187-192(1996). RN [3] RP VARIANTS CEP PHE-4; ARG-73 AND MET-228. RX MEDLINE; 92128898. RA BOULECHFAR S., DA SILVA V., DEYBACH J.-C., NORDMANN Y., GRANDCHAMP B., RA DE VERNEUIL H.; RL HUM. GENET. 88:320-324(1992). RN [4] RP VARIANTS CEP LEU-53 AND ARG-73. RX MEDLINE; 90234854. RA DEYBACH J.-C., DE VERNEUIL H., BOULECHFAR S., GRANDCHAMP B., RA NORDMANN Y.; RL BLOOD 75:1763-1765(1990). RN [5] RP VARIANTS CEP ALA-62; VAL-66; ARG-73 AND MET-228. RX MEDLINE; 92147890. RA WARNER C.A., YOO H.-W., ROBERTS A.G., DESNICK R.J.; RL J. CLIN. INVEST. 89:693-700(1992). RN [6] RP VARIANTS CEP CYS-19; PHE-82; ALA-99; VAL-104 AND SER-205. RX MEDLINE; 95164728. RA XU W., WARNER C.A., DESNICK R.J.; RL J. CLIN. INVEST. 95:905-912(1995). RN [7] RP VARIANT CEP PRO-212. RX MEDLINE; 96209895. RA TANIGAWA K., BENSIDHOUM M., TAKAMURA N., NAMBA H., YAMASHITA S., RA DE VERNEUIL H., GED C.; RL HUM. GENET. 97:557-560(1996). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER. CC -!- DISEASE: DEFECTS IN UROS ARE THE CAUSE OF CONGENITAL CC ERYTHROPOIETIC PORPHYRIA (CEP) (ALSO KNOWN AS GUENTHER'S DISEASE). CC THE MANIFESTATIONS OF CEP ARE HETEROGENEOUS, RANGING FROM CC NONIMMUNE HYDROPS FETALIS DUE TO SEVERE HEMOLYTIC ANEMIA IN UTERO CC TO MILDER, LATER ONSER FORMS, WHICH HAVE ONLY CUTANEOUS LESIONS IN CC ADULT LIFE. THE DEFIENCY IN UROS ACTIVITY RESULTS IN THE NON- CC ENZYMATIC CONVERSION OF HYDROXYMETHYLBILANE (HMB) INTO THE CC UROPORPHYRINOGEN-I ISOMER. DR EMBL; J03824; G337463; -. DR PIR; A40483; A40483. DR MIM; 263700; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; KW DISEASE MUTATION. FT ACT_SITE 148 148 POTENTIAL. FT VARIANT 4 4 L -> F (IN CEP). FT VARIANT 19 19 Y -> C (IN CEP). FT VARIANT 53 53 P -> L (IN CEP; NO DETECTABLE ACTIVITY; FT SEVERE PHENOTYPE). FT VARIANT 62 62 T -> A (IN CEP; NO DETECTABLE ACTIVITY). FT VARIANT 66 66 A -> V (IN CEP; RESIDUAL ACTIVITY; MILD FT PHENOTYPE). FT VARIANT 73 73 C -> R (IN CEP; NO DETECTABLE ACTIVITY; FT SEVERE PHENOTYPE). FT VARIANT 82 82 V -> F (IN CEP; HIGH RESIDUAL ACTIVITY; FT MILD PHENOTYPE). FT VARIANT 99 99 V -> A (IN CEP). FT VARIANT 104 104 A -> V (IN CEP; RESIDUAL ACTIVITY). FT VARIANT 212 212 S -> P (IN CEP; NO RESIDUAL ACTIVITY). FT VARIANT 225 225 G -> S (IN CEP). FT VARIANT 228 228 T -> M (IN CEP; NO DETECTABLE ACTIVITY). SQ SEQUENCE 265 AA; 28627 MW; E60CA8D8 CRC32; >HEM4_HUMAN MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLI FTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCG NAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNL NSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVS CTAESPTPQALATGIRKALQPHGCC


SWISSPROT:HEM4_ECOLI

ID HEM4_ECOLI STANDARD; PRT; 246 AA. AC P09126; DT 01-MAR-1989 (REL. 10, CREATED) DT 01-MAR-1989 (REL. 10, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)). GN HEMD. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12 / CS520; RX MEDLINE; 89041586. RA ALEFOUNDER P.R., ABELL C., BATTERSBY A.R.; RL NUCLEIC ACIDS RES. 16:9871-9871(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 88096587. RA JORDAN P.M., MGBEJE B.I.A., ALWAN A.F., THOMAS S.D.; RL NUCLEIC ACIDS RES. 15:10583-10583(1987). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 88134062. RA JORDAN P.M., MGBEJE B.I.A., THOMAS S.D., ALWAN A.F.; RL BIOCHEM. J. 249:613-616(1988). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE; 92358234. RA DANIELS D.L., PLUNKETT G. III, BURLAND V.D., BLATTNER F.R.; RL SCIENCE 257:771-778(1992). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER. DR EMBL; X12614; G41667; -. DR EMBL; Y00883; G41676; -. DR EMBL; M87049; G148203; -. DR PIR; S02227; S02227. DR PIR; S30694; S30694. DR ECOGENE; EG10430; HEMD. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT ACT_SITE 138 138 POTENTIAL. FT CONFLICT 236 236 A -> R (IN REF. 2 AND 3). SQ SEQUENCE 246 AA; 27798 MW; 74167D35 CRC32; >HEM4_ECOLI MSILVTRPSPAGEELVSRLRTLGQVAWHFPLIEFSPGQQLPQLADQLAALGESDLLFALS QHAVAFAQSQLHQQDRKWPRLPDYFAIGRTTALALHTVSGQKILYPQDREISEVLLQLPE LQNIAGKRALILRGNGGRELIGDTLTARGAEVTFCECYQRCAIHYDGAEEAMRWQAREVT MVVVTSGEMLQQLWSLIPQWYREHWLLHCRLLVVSERLAKLARELGWQDIKVADNADNDA LLRALQ


SWISSPROT:HEM4_BACSU

ID HEM4_BACSU STANDARD; PRT; 262 AA. AC P21248; DT 01-MAY-1991 (REL. 18, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) (UROS) (UROPORPHYRINOGEN- DE III COSYNTHETASE) (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)). GN HEMD. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91193218. RA HANSSON M., RUTBERG L., SCHROEDER I., HEDERSTEDT L.; RL J. BACTERIOL. 173:2590-2599(1991). RN [2] RP SEQUENCE OF 1-130 FROM N.A. RX MEDLINE; 90236876. RA PETRICEK M., RUTBERG L., SCHROEDER I., HEDERSTEDT L.; RL J. BACTERIOL. 172:2250-2258(1990). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = UROPORPHYRINOGEN-III CC + H(2)O. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). DR EMBL; M32130; -; NOT_ANNOTATED_CDS. DR EMBL; M57676; G143038; -. DR PIR; D35252; D35252. DR PIR; B42728; B42728. DR SUBTILIST; BG10343; HEMD. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT ACT_SITE 146 146 POTENTIAL. SQ SEQUENCE 262 AA; 29114 MW; F0AC476F CRC32; >HEM4_BACSU MENDFPLKGKTVLVTRNKAQAASFQQKVEALGGKAVLTSLITFRRALPNDVAEQVREDLA APGWLVFTSVNGADFFFSYLKENQLILPAHKKIAAVGEKTARRLKMHNVSVDVMPQEYIA EQLADALKQHAEPGETITVMKGNLSRDVIKQELVPLGFEVKEWVLYETIPDEEGIEALKD AAGQYSFDYVTFTSSSTVHTFMHVLGEELKKWKANGTACISIGPLTNDALLTYGITSHTP DTFTIDGMLELMCSMSREEERI


TREMBL:Q59683

ID Q59683 PRELIMINARY; PRT; 199 AA. AC Q59683; 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 UROPORPHYRINOGEN III SYNTHASE (EC 4.2.1.75) DE (UROPORPHYRINOGEN-III SYNTHASE) (UROPORPHYRINOGEN-III COSYNTHETASE) DE (UROPORPHYRINOGEN-III COSYNTHASE) (HYDROXYMETHYLBILANE HYDROLYASE DE (CYCLIZING)). GN HEMD. OS PROTEUS MIRABILIS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA TROTOT P., SISMEIRO O., VIVAR S.C., GLASER P., DANCHIN A.; RL SUBMITTED (APR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = CC UROPORPHYRINOGEN-III + H(2)O. DR EMBL; U22969; G726358; -. KW LYASE. SQ SEQUENCE 199 AA; 22799 MW; E6768384 CRC32; >Q59683 MSILITRPSPAGEQLTQRLIDAGKHAFHAPLIEIAAGKELSILENKLNKLSTGDYLFLLS KNAVWYANWQLNQLQQSWPDTLFYYGIGQSTAEEFQQLTAHSIRYPEFGETSEDLLALSS LQQIENKRVLLLRGNGGRELLATTLRQRGAIVDECECYQRLFIDYVSEEFALKWKNAQVE YLCGHQCEMLQQLLSSRWI


TREMBL:Q59335

ID Q59335 PRELIMINARY; PRT; 246 AA. AC Q59335; 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 UROPORPHYRINOGENIII COSYNTHASE (EC 4.2.1.75) DE (UROPORPHYRINOGEN-III SYNTHASE) (UROPORPHYRINOGEN-III COSYNTHETASE) DE (UROPORPHYRINOGEN-III COSYNTHASE) (HYDROXYMETHYLBILANE HYDROLYASE DE (CYCLIZING)). GN HEMD. OS CHLOROBIUM VIBRIOFORME. OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; GREEN BACTERIA; OC CHLOROBIACEAE. RN [1] RP SEQUENCE FROM N.A. RA MAJUMDAR D., WYCHE J.H.; RL SUBMITTED (DEC-1992) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = CC UROPORPHYRINOGEN-III + H(2)O. DR EMBL; M96364; G144480; -. KW LYASE. SQ SEQUENCE 246 AA; 26786 MW; 68C2910D CRC32; >Q59335 MKTVLVTRPKHQAAPFVRELEQYGLSTVVFPTIEIRPVAGWNVPDLTKFAGIFFTSPNSV QFFLKHLLQTAPDELKNLQQTRVWAVGKTTGQDLEKHGVSIEPLPKIADAVNLMADIDPA EIKGQTFLFVRGSLSLGTIPELIAEFGGTCVELTVYENLPPSLEDTQRVKDMLAEGKLDC LSFTSPSTAKNFFEAIGSKELSDSVQIAAIGTTTSGALEKMGIKVDIIPEYFDGPSFAKA IAEALK


TREMBL:Q59333

ID Q59333 PRELIMINARY; PRT; 60 AA. AC Q59333; 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 UROPORPHYRINOGEN III SYNTHASE (EC 4.2.1.75) DE (UROPORPHYRINOGEN-III SYNTHASE) (UROPORPHYRINOGEN-III COSYNTHETASE) DE (UROPORPHYRINOGEN-III COSYNTHASE) (HYDROXYMETHYLBILANE HYDROLYASE DE (CYCLIZING)) (FRAGMENT). GN HEMD. OS CHLOROBIUM VIBRIOFORME. OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; GREEN BACTERIA; OC CHLOROBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=F. THIOSULFATOPHILUM 8327; RA RHIE G., AVISSAR Y.J., BEALE S.I.; RL J. BIOL. CHEM. 271:8176-8182(1996). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = CC UROPORPHYRINOGEN-III + H(2)O. DR EMBL; U38348; G1033197; -. KW LYASE. FT NON_TER 1 1 SQ SEQUENCE 60 AA; 6279 MW; 808AE254 CRC32; >Q59333 STAKNFFEAIGSKELSDSVQIAAIGTTTSGALEKMGIKVDIIPEYFDGPSFAKAIAEALK


TREMBL:Q59294

ID Q59294 PRELIMINARY; PRT; 504 AA. AC Q59294; 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 UROPORPHYRINOGEN-III SYNTHASE (EC 4.2.1.75) DE (UROPORPHYRINOGEN-III COSYNTHETASE) (UROPORPHYRINOGEN-III COSYNTHASE) DE (HYDROXYMETHYLBILANE HYDROLYASE (CYCLIZING)). GN HEMD. OS CLOSTRIDIUM JOSUI. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FERM P-9684; RX MEDLINE; 95394829. RA FUJINO E., FUJINO T., KARITA S., OHMIYA K.; RL J. BACTERIOL. 177:5169-5175(1995). CC -!- CATALYTIC ACTIVITY: HYDROXYMETHYLBILANE = CC UROPORPHYRINOGEN-III + H(2)O. DR EMBL; D28503; G460693; -. KW LYASE. SQ SEQUENCE 504 AA; 55210 MW; E8349959 CRC32; >Q59294 MEHGFVALVGAGPGDKGLITIRGAELLSQADVVVYDRLVSQEIIKMIPTTAEKIDVGKEN KFHPVKQEEINHILLEKSLEGKKVIRLKGGDPFVFGRGGEELELLYENNIPFEVVPGVTS AVAALCYGGIPATHRDFCSSLHIITGHAREGGQLSIPFHELKELNGTIVFLMGDSSLSYL MNGLINAGMEKDMPAAIVENGTRPNQRKLVATVGTLEQKALEMEIKSPAIIAVGKVCSLS EKFSWFMKKPLFGTKILVTRPKESSGTLVEKLRQLGAEPVEYPCIEVVPIPQNEKLYHAC ENIREYGWILLTSKNGIQIFFDYLNSKGLDARVLANTKIGTVGSQTAKALKEVGLISDFT PEIFDGRHLALGIAERVGENEKVLICDAAIASDDIVNILRSNNIKFDRVPLYNTNYINEN SNKVKKSIVHGELKYITFTSASTVEGFIASMKDIPLESLTAVCIGNKTAEAAKKYNLRYV VAEKSTIDSMIDKLLEIGGGNIYD


TREMBL:Q47250

ID Q47250 PRELIMINARY; PRT; 246 AA. AC Q47250; 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 HEMD GENE ENCODING UROPORPHYRINOGEN-III COSYNTHETASE, DE COMPLETE CDS. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87308012. RA SASARMAN A., NEPVEU A., ECHELARD Y., DYMETRYSZYN J., DROLET M., RA GOYER C.; RL J. BACTERIOL. 169:4257-4262(1987). DR EMBL; M17360; G146336; -. SQ SEQUENCE 246 AA; 27768 MW; 2DE9E988 CRC32; >Q47250 MSILVTRPSPAGEELVSRLRTLGQVAWHFPLIEFSPGQQLPQLADQLAALGESDLLFALS QHAVAFAQSQLHQQDRKWPRLPDYFAIGRTTALALHTVSGQKILYPQDREISEVLLQLPE LQNIAGKRALILRGNGGRELIGDTLAARGAEVTFCECYQRCAIHYDGAEEAMRWQAREVT MVVVTSGEMLQQLWSLIPQWYREHWLLHCRLLVVSERLAKLARELGWQDIKVADNADNDA LLRALQ

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