ID A0A073KIU9_9BACI Unreviewed; 107 AA.
AC A0A073KIU9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Heme-degrading monooxygenase {ECO:0000256|HAMAP-Rule:MF_01272};
DE EC=1.14.14.18 {ECO:0000256|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme oxygenase {ECO:0000256|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-regulated surface determinant {ECO:0000256|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-responsive surface determinant {ECO:0000256|HAMAP-Rule:MF_01272};
GN Name=isdG {ECO:0000256|HAMAP-Rule:MF_01272};
GN ORFNames=BAGA_04210 {ECO:0000313|EMBL:KEK26450.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK26450.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK26450.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK26450.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) 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:0000256|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
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01272};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01272}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01272}.
CC -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC family. Heme-degrading monooxygenase IsdG subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01272}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01272}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEK26450.1}.
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DR EMBL; JOTM01000001; KEK26450.1; -; Genomic_DNA.
DR RefSeq; WP_033672827.1; NZ_LTAQ01000001.1.
DR AlphaFoldDB; A0A073KIU9; -.
DR STRING; 574375.AZF08_04255; -.
DR eggNOG; COG2329; Bacteria.
DR OrthoDB; 384737at2; -.
DR Proteomes; UP000027778; Unassembled WGS sequence.
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 Gene3D; 3.30.70.100; -; 1.
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 PANTHER; PTHR34474:SF4; HEME OXYGENASE (STAPHYLOBILIN-PRODUCING) 1; 1.
DR PANTHER; PTHR34474; SIGNAL TRANSDUCTION PROTEIN TRAP; 1.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR PROSITE; PS51725; ABM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01272};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01272};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01272};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01272};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01272};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01272}.
FT DOMAIN 2..93
FT /note="ABM"
FT /evidence="ECO:0000259|PROSITE:PS51725"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01272"
FT SITE 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01272"
SQ SEQUENCE 107 AA; 12175 MW; 75AEBD0C30A78E8D CRC64;
MIIVTNTSKI TKGDAHKLIE RFNKVGKVET MPGFLGLEVL LTENTVDYDE VTISTRWNSK
EDFQGWTKSN AFKDAHSHRS GLPEYIIENK ISFYDVKIVR MPIAAAQ
//
