(data stored in ACNUC29543 zone)

SWISSPROT: A5GRJ2_SYNR3

ID   A5GRJ2_SYNR3            Unreviewed;       410 AA.
AC   A5GRJ2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein {ECO:0000256|RuleBase:RU364116};
DE            EC=1.3.99.- {ECO:0000256|RuleBase:RU364116};
GN   Name=hemN {ECO:0000313|EMBL:CAK27501.1};
GN   OrderedLocusNames=SynRCC307_0598 {ECO:0000313|EMBL:CAK27501.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27501.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of porphyrin-containing
CC       compound. {ECO:0000256|RuleBase:RU364116}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU364116};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis. {ECO:0000256|RuleBase:RU364116}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III
CC       oxidase family. {ECO:0000256|RuleBase:RU364116}.
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DR   EMBL; CT978603; CAK27501.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0598; -.
DR   EnsemblBacteria; CAK27501; CAK27501; SynRCC307_0598.
DR   KEGG; syr:SynRCC307_0598; -.
DR   eggNOG; ENOG4105CSA; Bacteria.
DR   eggNOG; COG0635; LUCA.
DR   HOGENOM; HOG000015380; -.
DR   OMA; GPSAHSF; -.
DR   BioCyc; SSP316278:G1GJL-584-MONOMER; -.
DR   UniPathway; UPA00251; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.80.30.20; -; 1.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR004559; HemW-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR13932; PTHR13932; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00539; hemN_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRJ2.
DR   SWISS-2DPAGE; A5GRJ2.
KW   4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Iron {ECO:0000256|RuleBase:RU364116};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU364116};
KW   Metal-binding {ECO:0000256|RuleBase:RU364116};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364116,
KW   ECO:0000313|EMBL:CAK27501.1};
KW   Porphyrin biosynthesis {ECO:0000256|RuleBase:RU364116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN       10    238       Elp3. {ECO:0000259|SMART:SM00729}.
SQ   SEQUENCE   410 AA;  45138 MW;  BE5DD5636AE801C1 CRC64;
     MPLPAGRRPP RSLYLHIPFC HRRCFYCDFP VVPLGDQADG SRSQSIADYL HWLLRDLAAA
     PAGPPLSTVY IGGGTPSMLS PDQLAQLLAA VRSHWGLAPG AELTLEMDPA SFDRQRLEAV
     LALGINRVSL GGQSFDDAVL EQLGRRHRAN QLREACSWLR QAQQQTLLQS WSLDLIVNLP
     QQSFEAWDWE LSQALAQAPP HLSIYDLIVE PGTVFAWRQG RGELLLPDDD QAADRLQHTH
     QRLQAAGYGH YEVSSWALPG QASRHNRVYW SGASWWALGL GATSGVGTER LARPRTRDAY
     SEWVQADAGR QGDGPAAGWP PVEDLLLVGL RRREGVDLAW LHQTGLGGLE RAWLERVLAG
     WIERGVVELS AQRLRLVAPE GFSLSNAVLS DLLAALERSE PLAPTGARLG
//

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