HDOX2_STAAR
ID HDOX2_STAAR Reviewed; 108 AA.
AC Q6GKE0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Heme oxygenase (staphylobilin-producing) 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme-degrading monooxygenase 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-regulated surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-responsive surface determinant 2 {ECO:0000255|HAMAP-Rule:MF_01272};
GN Name=isdI; OrderedLocusNames=SAR0167;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39194.1; -; Genomic_DNA.
DR RefSeq; WP_000480605.1; NC_002952.2.
DR AlphaFoldDB; Q6GKE0; -.
DR SMR; Q6GKE0; -.
DR KEGG; sar:SAR0167; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; FRESHSH; -.
DR OrthoDB; 1562645at2; -.
DR Proteomes; UP000000596; 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..108
FT /note="Heme oxygenase (staphylobilin-producing) 2"
FT /id="PRO_0000270084"
FT DOMAIN 2..93
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 21..28
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 108 AA; 12790 MW; 8AFA59A571451E0A CRC64;
MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTKDTDE VKILTIWESE
DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
