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HDOX2_STAA8
ID   HDOX2_STAA8             Reviewed;         108 AA.
AC   Q2G1J2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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, ECO:0000269|PubMed:14570922};
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=SAOUHSC_00130;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14570922; DOI=10.1074/jbc.m307952200;
RA   Skaar E.P., Gaspar A.H., Schneewind O.;
RT   "IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus
RT   aureus.";
RL   J. Biol. Chem. 279:436-443(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       ECO:0000269|PubMed:14570922}.
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         ECO:0000269|PubMed:14570922};
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         ECO:0000269|PubMed:14570922};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC   -!- INDUCTION: Transcriptionally regulated by iron and the ferric uptake
CC       repressor (fur) protein. {ECO:0000305}.
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; CP000253; ABD29311.1; -; Genomic_DNA.
DR   RefSeq; WP_000480603.1; NZ_LS483365.1.
DR   RefSeq; YP_498730.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1J2; -.
DR   SMR; Q2G1J2; -.
DR   STRING; 1280.SAXN108_0151; -.
DR   EnsemblBacteria; ABD29311; ABD29311; SAOUHSC_00130.
DR   GeneID; 3919839; -.
DR   KEGG; sao:SAOUHSC_00130; -.
DR   PATRIC; fig|93061.5.peg.122; -.
DR   eggNOG; COG2329; Bacteria.
DR   HOGENOM; CLU_141544_2_1_9; -.
DR   OMA; FRESHSH; -.
DR   PRO; PR:Q2G1J2; -.
DR   Proteomes; UP000008816; 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   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..108
FT                   /note="Heme oxygenase (staphylobilin-producing) 2"
FT                   /id="PRO_0000270094"
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;  12791 MW;  8AF2718571451004 CRC64;
     MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE
     DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
 
 
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