ID   ODO1_BUCBP              Reviewed;         916 AA.
AC   Q89AJ7;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Oxoglutarate dehydrogenase;
DE            EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
GN   Name=sucA; OrderedLocusNames=bbp_280;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27005.1; -; Genomic_DNA.
DR   RefSeq; WP_011091406.1; NC_004545.1.
DR   AlphaFoldDB; Q89AJ7; -.
DR   SMR; Q89AJ7; -.
DR   STRING; 224915.bbp_280; -.
DR   KEGG; bab:bbp_280; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000000601; 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   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; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..916
FT                   /note="Oxoglutarate dehydrogenase"
FT                   /id="PRO_0000162189"
SQ   SEQUENCE   916 AA;  106047 MW;  9421601E0BE528CB CRC64;
     MYKNEFNSSW MSSFNSSYID NLYNKFLLDP TSIDNSWYIV FTELSKENYI NSTNKYLNNK
     FQDSKDTIKL TIELLINIFR TLGYKFAHLN PLDTFKNDNS LSLKKFLKSS EAFRIQDSYL
     VKLSQYVLDD ITTKNVYDDY KNIYCKRIGY QFMHIHNSNE MNWIKNYIET KHSNILKKKK
     KIQILKHLII SEMLEKYFSS KFPSIKRFSI EGAESLIPML KEVIKYTKKF NLHKIIFGMS
     HRGRLNVLAN ILDKPIKTIF NEFCENNSNN FNSGDVKYHM GFCCTKTIGL RKIILDLKSN
     PSHLEVINPV VVGSSRAYID SNDNLNDENI LPIIIHGDAA ISGQGVVQEL LNMSQARGYK
     VGGTIHIVVN NQIGFTTSKV KDLRTSQYCT DIAKMIDSPI FHVNADDPES VIFVTHLALN
     YRFCFKKDVF INLVCYRRHG HNEIDDPSIT QPVLYSKIKN HPTTATSYYN KLLLKNIINK
     SFLITYQKKI KKKLDVEYNL HNKKMSEKRL KCCSIVKADY INVSNTPINN ISQSDLTILA
     KKIFSIPNNI EVHNRVFKIY KDRLKMANNE KLFDWGASEL LAYASLLNEG ISCRLSGEDV
     CRGTFFHRHA VIHDQKNDSK YIPLKNIKLK QGNFYIWDSV LSEEATLAFE YGYSIDQKNT
     LNVWEAQFGD FANGAQIIID QFICSGEQKW NVTCNLVMLL PHGYEGQGPE HSSARIERYL
     QLSANNNIKI IIPTISSQIY HIIRKQAFSL IKKPLIIMSP KSLLRFPLAA SSLSELSNGK
     FRTVIDEIDN LDTKKVQRII LCSGKIYYDL LTQRRINQQK NIVILRIEQI YPRPTKKLSA
     ILYNYKDVHD YIWCQEEPCN QGAWLYHKSY LKKLLPKHSK LNYVGRSSSA SPATGYMKIH
     KEQQKKIIYD ALNISD
//