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Entry: Q64V18_BACFR
LinkDB: Q64V18_BACFR
Original site: Q64V18_BACFR 
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
//
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