ODO1_BRUA4
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 25-MAY-2022, entry version 87.
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; Proteobacteria; 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 / NBRC
RC 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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(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; Evidence={ECO:0000255|HAMAP-
CC 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 EnsemblBacteria; ABS13654; ABS13654; Oant_0933.
DR GeneID; 61318639; -.
DR KEGG; oan:Oant_0933; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 29166at2; -.
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 Gene3D; 3.40.50.11610; -; 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 PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
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
