ID   ODO1_AZOVI              Reviewed;         943 AA.
AC   P20707;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 91.
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; Synonyms=odhA;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2404759; DOI=10.1111/j.1432-1033.1990.tb15299.x;
RA   Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.;
RT   "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1.
RT   Molecular cloning and sequence analysis of the gene encoding the 2-
RT   oxoglutarate dehydrogenase component.";
RL   Eur. J. Biochem. 187:229-234(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.
RX   PubMed=2404760; DOI=10.1111/j.1432-1033.1990.tb15300.x;
RA   Westphal A.H., de Kok A.;
RT   "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2.
RT   Molecular cloning and sequence analysis of the gene encoding the
RT   succinyltransferase component.";
RL   Eur. J. Biochem. 187:235-239(1990).
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; X52433; CAA36680.1; -; Genomic_DNA.
DR   EMBL; X52432; CAA36677.1; -; Genomic_DNA.
DR   PIR; S07776; S07776.
DR   AlphaFoldDB; P20707; -.
DR   SMR; P20707; -.
DR   PRIDE; P20707; -.
DR   SABIO-RK; P20707; -.
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..943
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162186"
SQ   SEQUENCE   943 AA;  105688 MW;  D3F35356D454E2A1 CRC64;
     MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA EAGTSTDVPH
     APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI QAYRTRGHQA SQLDPLGLWQ
     RTAPSDLSIT HYGLTNADLD TPFRTGELYI GKEEATLREI LQALQETYCR TIGAEFTHIV
     DSEQRNWFAQ RLESVRGRPV YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES
     LVPVVDEIIQ RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD
     VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA TGEKVVPISI
     HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF TTSNPVDTRS TEYCTDPAKM
     IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY
     QKIAKQPTTR ELYADALVKE GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD
     WTPYLGHAWT ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN
     WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL QNLYEGQPKF
     ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG AQVVIDQFIS SGETKWGALC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP
     LVALTPKSLL RHKSAISTLE DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR
     HAEGREDIAI VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV
     ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV