ID   HDOX_BACC4              Reviewed;         107 AA.
AC   B7HF56;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Heme-degrading monooxygenase {ECO:0000255|HAMAP-Rule:MF_01272};
DE            EC=1.14.14.18 {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Heme oxygenase {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Iron-regulated surface determinant {ECO:0000255|HAMAP-Rule:MF_01272};
DE   AltName: Full=Iron-responsive surface determinant {ECO:0000255|HAMAP-Rule:MF_01272};
GN   Name=isdG {ECO:0000255|HAMAP-Rule:MF_01272};
GN   OrderedLocusNames=BCB4264_A4651;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
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: Allows bacterial pathogens to use the host heme as an iron
CC       source. Catalyzes the oxidative degradation of the heme macrocyclic
CC       porphyrin ring to the biliverdin in the presence of a suitable electron
CC       donor such as ascorbate or NADPH--cytochrome P450 reductase, with
CC       subsequent release of free iron. {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01272};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. Heme-degrading monooxygenase IsdG subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01272}.
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DR   EMBL; CP001176; ACK61348.1; -; Genomic_DNA.
DR   RefSeq; WP_000587818.1; NZ_VEHB01000006.1.
DR   AlphaFoldDB; B7HF56; -.
DR   SMR; B7HF56; -.
DR   EnsemblBacteria; ACK61348; ACK61348; BCB4264_A4651.
DR   GeneID; 67509183; -.
DR   KEGG; bcb:BCB4264_A4651; -.
DR   HOGENOM; CLU_141544_2_1_9; -.
DR   OMA; FRESHSH; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042167; P:heme catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR   HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR023953; IsdG.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..107
FT                   /note="Heme-degrading monooxygenase"
FT                   /id="PRO_1000140203"
FT   DOMAIN          2..94
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   BINDING         6
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   BINDING         76
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT   SITE            66
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
SQ   SEQUENCE   107 AA;  12034 MW;  E98EA5B28C19575C CRC64;
     MIIVTNTAKI TKGNGHKLIE RFNKVGKVET MPGFLGLEVL LTQNTVDYDE VTISTRWNAK
     EDFQGWTKSA AFKDAHSHQG GMPEYILDNK IAYYDVKVVR MPMAAAQ