GenomeNet

Database: UniProt
Entry: B7HGG1_BACC4
LinkDB: B7HGG1_BACC4
Original site: B7HGG1_BACC4 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system