ID A7GPL5_BACCN Unreviewed; 466 AA.
AC A7GPL5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, 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=Bcer98_1774 {ECO:0000313|EMBL:ABS22073.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS22073.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS22073.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS22073.1; -; Genomic_DNA.
DR RefSeq; WP_012094262.1; NC_009674.1.
DR AlphaFoldDB; A7GPL5; -.
DR STRING; 315749.Bcer98_1774; -.
DR GeneID; 56417349; -.
DR KEGG; bcy:Bcer98_1774; -.
DR eggNOG; COG1232; Bacteria.
DR HOGENOM; CLU_009629_3_0_9; -.
DR OMA; EHNQAVQ; -.
DR OrthoDB; 9805195at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002300; 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:ABS22073.1}.
FT DOMAIN 31..458
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 466 AA; 51970 MW; 3E1FA65D530CBA0C CRC64;
MKTVLVIGGG ITGLSTMFYL ERMKKDYNLD LNLILVEKEK YLGGKIHSVK KHGFIMETGA
DSMVARNEHV IPLIKELNLE EEMVYNETGI SYIYSDNMLH PIPADTVFGI PTSVESLFHS
TLVSAKGKIT ALKDFITKNK SFTKETSLAL FLESFLGKEL VEKQIAPVLS GVYSGKLHEL
TMASTLPYLV DYKNKYGSII KGFEVNKKQF QAAGNKKFVS FKNGLSTIIH RLEETLSDTE
IRKGMLTTNI SKNDDGYEVS FVNGETVKAD CVVLAVPHDV AQTILHSRDL DDEFDKFKNS
SLVSIYLGFD IPDHQLPADG TGFIVSENGN LQCDACTWTS RKWKHTSEKQ NLLVRMFYKS
SNANYEKMKH SSEEERLQIA LTDIEKSLGI QGKPQVVEVT NWDGLMPNYH LEHNQAVQSL
NEKLVKIVPN IYVAGASYYG VGIGACIGNG KQTASQIIKA LHNCSK
//