位置:首页 > 蛋白库 > HDOX_STAAB
HDOX_STAAB
ID   HDOX_STAAB              Reviewed;         107 AA.
AC   Q2YX89;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SAB1000;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ938182; CAI80688.1; -; Genomic_DNA.
DR   RefSeq; WP_000670950.1; NC_007622.1.
DR   AlphaFoldDB; Q2YX89; -.
DR   SMR; Q2YX89; -.
DR   KEGG; sab:SAB1000; -.
DR   HOGENOM; CLU_141544_2_1_9; -.
DR   OMA; VTIMTTW; -.
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)"
FT                   /id="PRO_0000270080"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024