ID   ODO1_BUCAP              Reviewed;         923 AA.
AC   Q8K9N3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=BUsg_292;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67847.1; -; Genomic_DNA.
DR   RefSeq; WP_011053814.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9N3; -.
DR   SMR; Q8K9N3; -.
DR   STRING; 198804.BUsg_292; -.
DR   EnsemblBacteria; AAM67847; AAM67847; BUsg_292.
DR   KEGG; bas:BUsg_292; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000000416; 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; Thiamine pyrophosphate.
FT   CHAIN           1..923
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162188"
SQ   SEQUENCE   923 AA;  107422 MW;  255A7653EED01A48 CRC64;
     MKKNTLEKWF NSSWLSGNNQ NYIEKIYESY LINPKSVDIT WQDKFSDLSK KRKNILKEEK
     FVYKNNSFKE IKIDKQEILE KKINYIINTF RKKGYKKSLI DPLKLNEQKK YKYLEPTFYH
     FSEDELKKTV KIDFKNSSQY EIKIRDLYEQ LNNKYCGSIG FEYMYIENSF EKKWITKHIE
     LFFKENLFIK KEKIRFLKEI LYGETFEKYL GKKFSGTKRF SLEGGETLIS ILHEIIRYSK
     KNDVSEIILG MAHRGRLNVL VNVLNKNPQV LFNEFSGINI PKEYSGDVKY HMGGITKIKN
     DKKKIYLKLA YNPSHLEIVN PVVLGIARAS INQLKISENK FLSINIHGDA SIIGQGVIQE
     TLNMSQTEAY KIGGTIHIVI NNQIGFTTSN PKNLRSSKYC TDVAKMIQAP VFHVNADDIE
     ASIFAIQLAL KFKKKFKKDV FIDLVCYRRH GHNEVDDPFV TQPIMYKKIH NHPTIGQIYS
     NLLISEKLIT SNDIEKIIEK YTTKLVQGKN VLSQERNITF QNGNKNFFIK KQKENTQLNF
     LNIKDLLYSI NTIPNSIEVH NRVKKIYQER IGMADGQILL DWGTAELLAY ATILKEGISC
     RLSGEDISRG TFFHRHAFIH DQNNGSIYVP LQNIEKNQGK FEIWDSVLSE EAVLAFEYGY
     SLFPSNNLTI WEAQFGDFAN GAQVVIDQFI SSSEQKWNQK SNLVLFLPHG YEGQGPEHSS
     ARLERFLQLC AENNIQVCIP TVSSQIFHLL RRQIFSNVYK PLIVLTPKSL LRNNVARSSL
     EVLVNENFKN VINEIDKNQK EVKRIIFCSG KIYYDLLEYR NKCDINNVLL IRIEQLYPFP
     KDEILTILKS YSYVQDFIWC QEEPHNQGAW FYIKDLLSTL LPLNSHLNYV SRPSAASPAA
     GHILIHRKEQ EKLINNAFNF KIA