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 27-NOV-2024, entry version 121.
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; Pseudomonadota; 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=N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = N(6)-[(R)-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; 563178.BUAP5A_296; -.
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 Proteomes; UP000001806; 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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:TreeGrafter.
DR CDD; cd02016; TPP_E1_OGDC_like; 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 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; 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
//
