ID   ODO1_BUCAI              Reviewed;         909 AA.
AC   P57388;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; OrderedLocusNames=BU302;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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:0000250|UniProtKB:P0AFG3}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
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:0000250|UniProtKB:P0AFG3}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB13011.1; -; Genomic_DNA.
DR   RefSeq; NP_240125.1; NC_002528.1.
DR   RefSeq; WP_010896057.1; NC_002528.1.
DR   AlphaFoldDB; P57388; -.
DR   SMR; P57388; -.
DR   STRING; 107806.10038976; -.
DR   PRIDE; P57388; -.
DR   EnsemblBacteria; BAB13011; BAB13011; BAB13011.
DR   KEGG; buc:BU302; -.
DR   PATRIC; fig|107806.10.peg.313; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OMA; RDSYCRT; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.50.11610; -; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
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; PF16078; 2-oxogl_dehyd_N; 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; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..909
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162187"
SQ   SEQUENCE   909 AA;  105807 MW;  AE739F8CD9F9CF8B CRC64;
     MDKNKIEYWL NSSWLSRENQ NYIETIYKSF LTNAQSIDDM WHKAFLEFSE EQKNTYERNN
     TKNNKYLLIK KIDHMIHAFR SEGYQQSLID PLKLKKRTKI HDLDLSFYNF TEEETRQTVE
     INFKNCTNFR TNIISLYKIL YKKYCGSIGF EYMYVNNLLE KQWITNHIES FFNENVFTIE
     EKINFLKELT YAETLEKYIG KKFPGAKRFS LEGAETLIPV LHEVIRFSKK NNISKIVLGM
     AHRGRLNVLI NVLNKSPKVL FDEFSNLNLF QKISGDVKYH MGGTAEIQYE KKIIFHMACN
     PSHLEIINPV VSGISRSYID NMKNIDNEVL PISIHGDASV IGQGVVQETL NMSQTEGYKV
     GGTVHIIINN QIGFTTSNPK HLRSSEYCTD VAKIIQAPVF HVNADDLEAS IFAIQLALHF
     RKIFKKDVFI DLVCYRRNGH NEVDEPSVTQ PIMYQKIKNH PTSRTIYSDV LISKKIITSE
     KNQEIMNQYL SKLQKGHYIF SKSKNIHFKN EFFLEEKKIK KIKKDVNFSD LKNLACLINQ
     IPDSVKMHQR VKKIYEERLE MAQRLKLFDW GAAETLAYAT ILNEGISCRI SGEDVSRGTF
     FHRHAFIHNQ INGSIYIPLN NISKKQGKFQ IWDSVLSEEA VLAFEYGYSL SSPNTLTIWE
     AQFGDFINGA QIVIDQFISS GEQKWNKKSN LVVLLPHGYE GQGPEHSSSR IERFLQLCAE
     ENMQICIPTT SSQIFHIFRK QIFDKILKPL IIFTPKSLLR NPMASSSFDD LVYGKFQKIL
     DEVDNVNKKE IRLIFCSGKI YYDLLRNRRE KKINSIILIR IEQLYPFPEG EILKILKNYF
     YIKDFIWCQE EPYNQGAWFY IKDCLSNILP LDASLKYIGR SSSASPAVGY ISIHKKQQEK
     IIYNALNIN