ID   C1DM56_AZOVD            Unreviewed;       943 AA.
AC   C1DM56;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 76.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:ACO79143.1};
GN   OrderedLocusNames=Avin_29770 {ECO:0000313|EMBL:ACO79143.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO79143.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO79143.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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:0000256|ARBA:ARBA00003906}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051911};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:0000256|ARBA:ARBA00011301}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; CP001157; ACO79143.1; -; Genomic_DNA.
DR   RefSeq; WP_012701530.1; NC_012560.1.
DR   AlphaFoldDB; C1DM56; -.
DR   STRING; 322710.Avin_29770; -.
DR   EnsemblBacteria; ACO79143; ACO79143; Avin_29770.
DR   GeneID; 309096903; -.
DR   KEGG; avn:Avin_29770; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
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:0006099; P:tricarboxylic acid cycle; IEA:TreeGrafter.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   FunFam; 1.10.287.1150:FF:000004; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.12470:FF:000009; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   FunFam; 3.40.50.970:FF:000014; 2-oxoglutarate dehydrogenase E1 component; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002424};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..792
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   943 AA;  105874 MW;  E7E07FEB527E01F8 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 EAQFGDFANG AQVVIDQFIS SGETKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP
     LVALTPKSLL RHKSAISTLE DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR
     HAEGREDIAI VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV
     ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV
//