ID K2GJK7_9BACI Unreviewed; 954 AA.
AC K2GJK7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN ORFNames=MJ3_12350 {ECO:0000313|EMBL:EKE30619.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE30619.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE30619.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE30619.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_01169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE30619.1}.
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DR EMBL; AMPQ01000043; EKE30619.1; -; Genomic_DNA.
DR RefSeq; WP_008592174.1; NZ_CP011361.2.
DR AlphaFoldDB; K2GJK7; -.
DR STRING; 1230341.AAV35_009805; -.
DR PATRIC; fig|1230341.3.peg.2490; -.
DR eggNOG; COG0567; Bacteria.
DR Proteomes; UP000011746; Unassembled WGS sequence.
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 HAMAP; MF_01169; SucA_OdhA; 1.
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; 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 {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01169}; Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 596..792
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 954 AA; 108122 MW; 9FE0C3E4A1BDF874 CRC64;
MSNTESKVSF WSNFHGPNMG YIEEQYERFQ EDENAVDASM KELFEKHGAP VESERPAAES
SGGNVPSAQD VSKIAAALKL VEAIRRDGHL SADIYAVGGF DRPDTELLEP ETYGISKEDL
EQLPAEWIWP EANVKLNNAW QAIETLKERY AGTLSFEYEH VHNERERSWL KERIESGSYS
VNLSTEERKQ LLYRLIEVEN FEQFLGKTFV AQKRFSIEGM DAMVPMLDKI VQSAAVDHIQ
HVMLGMAHRG RLNVLAHVLG KPYEKIFSEF NHSPEKELMP SEGSQGINYG WTGDVKYHFG
AKREVKNGDD SHATRVTLSH NPSHLEFVNP VVQGFTRAAQ DYREERGNSV IDEDAALGVL
IHGDAAFIGE GIVAETLNLS DLEGYRSGGT VHIIANNLVG FTTNRKDGRS TRYASDLAKG
FEIPIMHVNA DDPEACLSAI ALAYEYRQTF HKDVLIDLVG YRRYGHNEID EPRATQPRLY
SEIDEHPTIA NVYGENLLNQ GVIQDGELDE YKEKATSNLR DIYNSMKEEE TYEPDVQGRP
QGVERSLEEF ETVVDLDRLK TLNKQMLERP EGFNGFKKLE KILNKRENML EEGNKVDWAT
AEALAFASIL EEGQPIRVTG QDTERGTFAH RHMVLHDVET GETYCPLHGI EQAKASFDIF
NSPLSEAGVL GFEYGYSVHS QETLVVWEAQ FGDFANAGQV IFDQFVSSGR AKWNEQSNMV
FLLPHGYEGQ GPEHSSARLE RFLQMSAENN WTVANVTSAA QYFHLLRRQS AISCKEEERP
LVLMTPKSLL RNQRVASEAK EFTDSGFHPL VRQPGLTKTK KKDKSKVKTL LLGSGKIMVD
IEDRTEQEES SFETIDAVRV EQIYPFPDQK LKEIMKEYPN LKELVWVQEE PQNMGSWYFV
EGILYNLLEE GQIHRYVGRP HRASPSVGEP NIHKTEQNRI IKEALQISKG GNSQ
//
