HDOX1_STAAW
ID HDOX1_STAAW Reviewed; 107 AA.
AC Q8NX62;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=MW1018;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF ASN-7; LYS-17; PHE-23; MET-38; TRP-67; SER-70 AND HIS-77.
RX PubMed=15520015; DOI=10.1074/jbc.m409526200;
RA Wu R., Skaar E.P., Zhang R., Joachimiak G., Gornicki P., Schneewind O.,
RA Joachimiak A.;
RT "Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with
RT structural similarity to monooxygenases.";
RL J. Biol. Chem. 280:2840-2846(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 ECO:0000269|PubMed:15520015}.
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 ECO:0000269|PubMed:15520015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC -!- MISCELLANEOUS: IsdG seems to carry out oxygenation of the heme without
CC the assistance of any of the prosthetic groups or cofactors normally
CC associated with activation of molecular oxygen.
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; BA000033; BAB94883.1; -; Genomic_DNA.
DR RefSeq; WP_000670950.1; NC_003923.1.
DR PDB; 1XBW; X-ray; 1.90 A; A/B/C/D=1-107.
DR PDBsum; 1XBW; -.
DR AlphaFoldDB; Q8NX62; -.
DR SMR; Q8NX62; -.
DR EnsemblBacteria; BAB94883; BAB94883; BAB94883.
DR KEGG; sam:MW1018; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR OMA; VTIMTTW; -.
DR BRENDA; 1.14.99.48; 3352.
DR EvolutionaryTrace; Q8NX62; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase.
FT CHAIN 1..107
FT /note="Heme oxygenase (staphylobilin-producing) 1"
FT /id="PRO_0000270089"
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"
FT MUTAGEN 7
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 17
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 23
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 38
FT /note="M->A: Slight loss of activity. Changes in heme
FT binding."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 67
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 70
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:15520015"
FT MUTAGEN 77
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15520015"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1XBW"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:1XBW"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1XBW"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1XBW"
FT STRAND 47..60
FT /evidence="ECO:0007829|PDB:1XBW"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:1XBW"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:1XBW"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1XBW"
FT STRAND 91..106
FT /evidence="ECO:0007829|PDB:1XBW"
SQ SEQUENCE 107 AA; 12546 MW; DB13A134D5EC4FF0 CRC64;
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK
