ODO1_STAA1
ID ODO1_STAA1 Reviewed; 932 AA.
AC A7X295; Q7ASB7; Q7WRM3; Q7WRN1; Q7WRX0; Q7WZ40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169}; OrderedLocusNames=SAHV_1401;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P.,
RA Walsh T.R.;
RT "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced
RT susceptibility to vancomycin (VRSA) and hetero-VRSA (hVRSA).";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000255|HAMAP-Rule:MF_01169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000255|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR EMBL; AJ564530; CAD92197.1; -; Genomic_DNA.
DR EMBL; AP009324; BAF78284.1; -; Genomic_DNA.
DR RefSeq; WP_000180673.1; NC_009782.1.
DR AlphaFoldDB; A7X295; -.
DR SMR; A7X295; -.
DR KEGG; saw:SAHV_1401; -.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OMA; RDSYCRT; -.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.50.11610; -; 1.
DR HAMAP; MF_01169; SucA_OdhA; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 3: Inferred from homology;
KW Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..932
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000313016"
FT CONFLICT 46
FT /note="T -> I (in Ref. 1; CAD92197)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="N -> K (in Ref. 1; CAD92197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 932 AA; 105357 MW; F671CE1A65ADAF6D CRC64;
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND DSIVPALKST
SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV PKLEIEDFDL DQQTLEGISA
GIVSDHFADI YDNAYEAILR MEKRYKGPIA FEYTHINNNT ERGWLKRRIE TPYKVTLNNN
EKRALFKQLA YVEGFEKYLH KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM
AHRGRLNVLT HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD
SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP IIIHGDAAYP
GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA RSTTYSTDVA KGYDVPIFHV
NADDVEATIE AIDIAMEFRK EFHKDVVIDL VGYRRFGHNE MDEPSITNPV PYQNIRKHDS
VEYVFGKKLV NEGVISEDEM HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ
ADEQSFTFDH LKEINDALLT YPDGFNILKK LNKVLEKRHE PFNKEDGLVD WAQAEQLAFA
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPDQKATF DIHNSPLSEA
AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF SSRSKWGERS GLTLFLPHAY
EGQGPEHSSA RLERFLQLAA ENNCTVVNLS SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK
SLLRNKTVAK PIDEFTSGGF EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL
LVAIERLYPF PEEEIEALLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN
