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
//