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 27-MAR-2024, entry version 115.
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; Pseudomonadota; 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=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, 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 GeneID; 75258829; -.
DR KEGG; bas:BUsg_292; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
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 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; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
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; 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
//
