ID   ODO1_BRUA4              Reviewed;        1001 AA.
AC   A6WXF0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=sucA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Synonyms=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=Oant_0933;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 /
RC   NBRC 15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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:0000255|HAMAP-Rule:MF_01169}.
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:0000255|HAMAP-Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
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:0000255|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR   EMBL; CP000758; ABS13654.1; -; Genomic_DNA.
DR   RefSeq; WP_010657592.1; NC_009667.1.
DR   AlphaFoldDB; A6WXF0; -.
DR   SMR; A6WXF0; -.
DR   STRING; 439375.Oant_0933; -.
DR   GeneID; 61318639; -.
DR   KEGG; oan:Oant_0933; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   PhylomeDB; A6WXF0; -.
DR   Proteomes; UP000002301; Chromosome 1.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
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..1001
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_1000065701"
SQ   SEQUENCE   1001 AA;  112439 MW;  FEFF96316C9AC4AB CRC64;
     MARQEQANDV FALTSFLYGG NADYIEELYA KYEDDPNSVD PQWRDFFAKL GDNADDVKKN
     AEGASWTRKN WPIAANGELI SALDGNWAEV EKHVTDKLKG KAAKGEAKGA TGAALTSEEI
     TQAARDSVRA IMMIRAYRMR GHLHANLDPL GLSEKPNDYN ELEPENYGFT PADYNRKIFI
     DNVLGLEYAT VPEMLDILKR TYCGTIGVEF MHISDPAEKA WIQERIEGPD KKVAFTPEGK
     KAILSKLIEA EGFEQFIDVK YKGTKRFGLD GGESLIPALE QIVKRGGAMG VKEIIFGMAH
     RGRLNVLSQV MGKPHRAIFH EFKGGSYAPD DVEGSGDVKY HLGASSDREF DGNKVHLSLT
     ANPSHLEIVN PVVMGKARAK QDLLAGRTRD DMVPLATRAK VLPLLLHGDA AFAGQGVVAE
     CLGLSGLKGH RVAGTLHFII NNQIGFTTNP AFSRSSPYPS DVAKMIEAPI FHVNGDDPEA
     VVFAAKVATE FRMTFHKPVV IDMFCYRRFG HNEGDEPSFT QPLMYKAIRA HKTTVQLYSD
     KLIAEGLIKQ EEIDQMKAQW RENLETEFDA GQSYKPNKAD WLDGAWAGLR TADNADEQRR
     GKTAVPMKTL KEIGKKLVEV PKDFHVHRTI QRFLDNRAKM METGEGIDWA TAESLAFGSL
     VAEGSPIRLS GQDVERGTFS QRHTVLYDQE TQNRYIPLNN IQKGQAIYEA INSMLSEEAV
     LGYEYGYSLS DPRALVLWEA QFGDFANGAQ VVFDQFISSG ERKWLRMSGL VCLLPHGYEG
     QGPEHSSARL ERWLQMCAED NMQVANVTTP ANYFHILRRQ MKRDFRKPLI MMTPKSLLRH
     KRAVSTLNEL SGESSFHRLL WDDAQYNKDE GIKLQKDAKI RRVVLCSGKV YYDLYEEREK
     RGIDDVYLLR VEQLYPFPAK ALINELSRFR HAEMVWCQEE PKNMGAWSFI DPYLEWVLAH
     IDAKHQRVRY AGRPAAASPA TGLMSKHLAQ LAAFLEDALG N
//