ID   HDOX_STAS1              Reviewed;         104 AA.
AC   Q49ZB8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=SSP0713;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17858.1; -; Genomic_DNA.
DR   RefSeq; WP_011302628.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q49ZB8; -.
DR   SMR; Q49ZB8; -.
DR   STRING; 342451.SSP0713; -.
DR   EnsemblBacteria; BAE17858; BAE17858; SSP0713.
DR   KEGG; ssp:SSP0713; -.
DR   PATRIC; fig|342451.11.peg.715; -.
DR   eggNOG; COG2329; Bacteria.
DR   HOGENOM; CLU_141544_2_1_9; -.
DR   OMA; FEAWRNS; -.
DR   OrthoDB; 1562645at2; -.
DR   Proteomes; UP000006371; 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;
KW   Reference proteome.
FT   CHAIN           1..104
FT                   /note="Heme oxygenase (staphylobilin-producing)"
FT                   /id="PRO_0000270100"
FT   DOMAIN          2..95
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;  11938 MW;  B5035B56D651A8FE CRC64;
     MYVVTNRIDV KKGFAEKMAP KFTQGGKIQE LEGFQKVEVW LIDDEADYDQ MYINTWWDSE
     DDFKGWLKSD AFKEAHEGKS KTKSDDSPIL GNKVVKANVI SELS