ID   ODO1_STAAB              Reviewed;         932 AA.
AC   Q2YY05;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=SAB1269c;
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: 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; AJ938182; CAI80958.1; -; Genomic_DNA.
DR   RefSeq; WP_000180686.1; NC_007622.1.
DR   AlphaFoldDB; Q2YY05; -.
DR   SMR; Q2YY05; -.
DR   KEGG; sab:SAB1269c; -.
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_1000065704"
SQ   SEQUENCE   932 AA;  105364 MW;  A8642ACB91D4A5B0 CRC64;
     MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND DSIVPSLKST
     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 IIIHGDGAYP
     GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA RSTTYSTDVA KGYDVPIFHV
     NADDVEATIE AIDIAMEFRK EFHKDVVIDL VGYRRFGHNE MDEPSITNPV PYQNIRKNDS
     VEYVFGKKLV NEGVISEDEM HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ
     ADEQSFTFDH LKEINDALLT YPDGFNILKK LNKVLKKRHE PFNKEDGLVD WAQAEQLAFA
     TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPNQKATF DIHNSPLSEA
     AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF SSRSKWGERS GLTLFLPHAY
     EGQGPEHSSA RLERFLQLAA ENNCTVVNLS SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK
     SLLRNKTVAK PIDEFTSGGF EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL
     LVAIERLYPF PEEEIETLLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY
     HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN