HDOX_STAHJ
ID HDOX_STAHJ Reviewed; 104 AA.
AC Q4L849;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Heme oxygenase (staphylobilin-producing) {ECO:0000255|HAMAP-Rule:MF_01272};
DE EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme-degrading monooxygenase {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; OrderedLocusNames=SH0867;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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 oxo-bilirubin chromophore staphylobilin (a
CC mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-
CC beta-bilirubin) in the presence of a suitable electron donor such as
CC ascorbate or NADPH--cytochrome P450 reductase, with subsequent release
CC of free iron. {ECO:0000255|HAMAP-Rule:MF_01272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37039,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74361;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37363,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74362;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-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; AP006716; BAE04176.1; -; Genomic_DNA.
DR RefSeq; WP_011275179.1; NC_007168.1.
DR AlphaFoldDB; Q4L849; -.
DR SMR; Q4L849; -.
DR STRING; 279808.SH0867; -.
DR EnsemblBacteria; BAE04176; BAE04176; SH0867.
DR GeneID; 58062956; -.
DR KEGG; sha:SH0867; -.
DR eggNOG; COG2329; Bacteria.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; FEAWRNS; -.
DR OrthoDB; 1562645at2; -.
DR Proteomes; UP000000543; 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..104
FT /note="Heme oxygenase (staphylobilin-producing)"
FT /id="PRO_0000270099"
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 104 AA; 12025 MW; 9BF949E5DAE814A4 CRC64;
MFVVTNRITV KKGFAEKMAP RFTKGGKIEA LQGFHKIEVW KVTRDHENED MYVNTWWETE
KDFEAWTKSD AFKEAHQNRD KTSSESSPVI SSEIVKATVL STLN
