ID B7HGG1_BACC4 Unreviewed; 473 AA.
AC B7HGG1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000256|RuleBase:RU364052};
DE EC=1.3.3.15 {ECO:0000256|RuleBase:RU364052};
GN Name=hemY1 {ECO:0000313|EMBL:ACK61509.1};
GN OrderedLocusNames=BCB4264_A1105 {ECO:0000313|EMBL:ACK61509.1};
OS Bacillus cereus (strain B4264).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK61509.1, ECO:0000313|Proteomes:UP000007096};
RN [1] {ECO:0000313|EMBL:ACK61509.1, ECO:0000313|Proteomes:UP000007096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4264 {ECO:0000313|EMBL:ACK61509.1,
RC ECO:0000313|Proteomes:UP000007096};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus B4264.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001176; ACK61509.1; -; Genomic_DNA.
DR RefSeq; WP_001228101.1; NC_011725.1.
DR AlphaFoldDB; B7HGG1; -.
DR KEGG; bcb:BCB4264_A1105; -.
DR HOGENOM; CLU_009629_3_0_9; -.
DR OMA; WFDQWFG; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000007096; 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:ACK61509.1}.
FT DOMAIN 12..459
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 473 AA; 52525 MW; 4EC5CA986948D3DC CRC64;
MRKKVVIVGG GITGLTAMYN LQKNIHEKNL PIDTLLIEAS GKLGGKIQTV RKDGFTIERG
PDSFLARKES AARLVKELGL GDELVNNQAG QSFILVNNRL HKMPNGSMMG IPTQITPFLF
SGLFSPIGKL RAGFDLLMPR SKPVSDQSLG QFFRHRLGNE VVENLIEPLL SGIYAGDIDE
MSLMSTFPQM YQIEQKHRSI SLGMRTLAPK EEKAEPKKGM FQTVKTGLES IVKSLEAKMH
EGTIIKGTRI EKVAKQGDGY TITLSNGKEI EADAIVVATS HKVLPSMFAQ YKQFRFFRNI
PSTSVANVAL AFQKSAIQRD INGTGFVVSR NSDYTITACT WTHKKWPHTT PEGKTLLRCY
VGRAGDEAVV EQTEEELVQL VLEDLRKTMD ITEDPEFTIV SRWKEAMPQY TVGHNERMKK
LTTFMEKELP GIYLAGSSYA GAGLPDCMNQ GEEAAKRVLS HLEKVIDAEL IAQ
//