ID Q64V18_BACFR Unreviewed; 462 AA.
AC Q64V18;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN OrderedLocusNames=BF1913 {ECO:0000313|EMBL:BAD48661.1};
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD48661.1, ECO:0000313|Proteomes:UP000002197};
RN [1] {ECO:0000313|EMBL:BAD48661.1, ECO:0000313|Proteomes:UP000002197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD48661.1,
RC ECO:0000313|Proteomes:UP000002197};
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC III. {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|RuleBase:RU364052};
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|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|RuleBase:RU364052}.
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DR EMBL; AP006841; BAD48661.1; -; Genomic_DNA.
DR RefSeq; WP_011202640.1; NC_006347.1.
DR RefSeq; YP_099195.1; NC_006347.1.
DR AlphaFoldDB; Q64V18; -.
DR STRING; 295405.BF1913; -.
DR KEGG; bfr:BF1913; -.
DR PATRIC; fig|295405.11.peg.1860; -.
DR HOGENOM; CLU_009629_3_0_10; -.
DR OMA; WFDQWFG; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002197; 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:SF40; LYSINE-SPECIFIC HISTONE DEMETHYLASE 2; 1.
DR PANTHER; PTHR42923; 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}.
FT DOMAIN 21..441
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 462 AA; 50923 MW; 220F4A0D228803D5 CRC64;
MNQTVTENHR LRDTIIIGAG LTGLTTAYCL TRKGCDIEVI EQSPCVGGQI RTYHENGFTF
ESGPNTGVIS HPEVAELLAE LSPTCRLETA SEASRQRLIW KGDRFHSLPS GLFSAITTPL
FSTKDKFNIL GEPFRAKGNN PDETIGELVQ RRLGISYLHY AVDPFISGVY AGDPMRLVTR
HALPKLYQLE QTYGSFILGG IAKSFSHRSE RDRLATRKVF STYGGLSNLT KALEQAIGIK
RFSLGATSTS LMPCEQGWVV SFTDSCGIVN RIHCRKVITT APAFALPSLL PFVPDKQMNR
ISNLTYAPVM QVSVGLRNTY GKEFHAFGGL VPSCEQKPVL GILFPSACFD NRSPEGGALY
SYFLGGTRHP ELLEKSDDEI IRLITTGLNE MLDYPAGIVP DLIRIFRHKK AIPQYESSST
DRFAAINELQ KQYPGLVVAG NLKGGIGMAD RIKQAVEIAR ER
//