HDOX1_STAAC
ID HDOX1_STAAC Reviewed; 107 AA.
AC Q5HGU8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Heme oxygenase (staphylobilin-producing) 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme-degrading monooxygenase 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-regulated surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-responsive surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
GN Name=isdG; OrderedLocusNames=SACOL1146;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000046; AAW38025.1; -; Genomic_DNA.
DR RefSeq; WP_000670950.1; NC_002951.2.
DR AlphaFoldDB; Q5HGU8; -.
DR SMR; Q5HGU8; -.
DR EnsemblBacteria; AAW38025; AAW38025; SACOL1146.
DR KEGG; sac:SACOL1146; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; VTIMTTW; -.
DR Proteomes; UP000000530; 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 oxygenase (staphylobilin-producing) 1"
FT /id="PRO_0000270081"
FT DOMAIN 3..92
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT BINDING 7
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT BINDING 22..29
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT BINDING 77
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 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
SQ SEQUENCE 107 AA; 12546 MW; DB13A134D5EC4FF0 CRC64;
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK
