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Database: UniProt
Entry: F2RAP9_STRVP
LinkDB: F2RAP9_STRVP
Original site: F2RAP9_STRVP 
ID   F2RAP9_STRVP            Unreviewed;       499 AA.
AC   F2RAP9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|ARBA:ARBA00019046, ECO:0000256|RuleBase:RU364052};
DE            EC=1.3.3.15 {ECO:0000256|ARBA:ARBA00012402, ECO:0000256|RuleBase:RU364052};
GN   OrderedLocusNames=SVEN_5832 {ECO:0000313|EMBL:CCA59118.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59118.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA59118.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC       III. {ECO:0000256|ARBA:ARBA00002185, ECO:0000256|RuleBase:RU364052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2;
CC         Xref=Rhea:RHEA:43436, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57309, ChEBI:CHEBI:131725; EC=1.3.3.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001755};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC         Evidence={ECO:0000256|ARBA:ARBA00001755};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU364052};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004744,
CC       ECO:0000256|RuleBase:RU364052}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364052}.
CC   -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC       oxidase family. Coproporphyrinogen III oxidase subfamily.
CC       {ECO:0000256|ARBA:ARBA00008310, ECO:0000256|RuleBase:RU364052}.
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DR   EMBL; FR845719; CCA59118.1; -; Genomic_DNA.
DR   RefSeq; WP_015037013.1; NZ_JABVZO010000442.1.
DR   AlphaFoldDB; F2RAP9; -.
DR   STRING; 953739.SVEN_5832; -.
DR   GeneID; 69867882; -.
DR   KEGG; sve:SVEN_5832; -.
DR   PATRIC; fig|953739.5.peg.1045; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_009629_3_1_11; -.
DR   OMA; EHNQAVQ; -.
DR   OrthoDB; 4496419at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   NCBIfam; TIGR00562; proto_IX_ox; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364052};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU364052};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU364052};
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW   ECO:0000256|RuleBase:RU364052};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364052,
KW   ECO:0000313|EMBL:CCA59118.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          21..472
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   499 AA;  50358 MW;  CA027A2F423DFDD8 CRC64;
     MNADTTGQHA VPHVVVVGGG IAGLAAAHRL AHAGHRVTLL EADDRLGGKL LAGEIAGAPV
     DLGAESLLAR RPEAVSLARA VGLGDRLQAP ATTTASVWSR GELVPMPKGH VMGVPGTPEA
     VEGLLSAEGV RRIGGDLELP PTEIGDDIAI GAYVAARMGH EVVDRLVEPL LGGVYAGDAH
     RISMKAAVPA LFEAARAHPT LTAAVHAVQR AGAATPADAA GAANGLGGSV FLGIEGGIGT
     LPGAVADAVR TAGGEVLTGV PVQTLVRSGA TGWQVVTRHR TFDADAVVLA TPAGVAAALV
     GGHAPAAGAE LDAIDYASMA LVTLAFRRSD MPELAGSGFL VPPVDGHTVK ASTFSSQKWR
     WVSDGAPGLF VLRTSVGRHG EEEQVHREDS DLVAASLKDL AAATGLAAHP VASTVTRWIG
     GLPQYPVGHL DRVARIRAGV AALPGLRLAG AAYDGVGIPA CISSAHRAAD EIAGELARRR
     GEEIIATSKT GDPGAGHSL
//
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