ID Q9KQB3_VIBCH Unreviewed; 936 AA.
AC Q9KQB3;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=VC_2087 {ECO:0000313|EMBL:AAF95233.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF95233.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF95233.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; AE003852; AAF95233.1; -; Genomic_DNA.
DR PIR; B82121; B82121.
DR RefSeq; NP_231719.1; NC_002505.1.
DR RefSeq; WP_000551472.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KQB3; -.
DR STRING; 243277.VC_2087; -.
DR DNASU; 2613343; -.
DR EnsemblBacteria; AAF95233; AAF95233; VC_2087.
DR GeneID; 69719290; -.
DR KEGG; vch:VC_2087; -.
DR PATRIC; fig|243277.26.peg.1994; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 936 AA; 105320 MW; F6EA661CD253245C CRC64;
MHNGVMKAWL ESSHLAGANA TYVEDLYELY LSDPDLVSEE WKRVFDGLPA HPTNVVEQPH
SRVRDYFRRL AQETKHYNVQ VSDPEVDAKQ VKVLQLINAY RFRGHEAAKL DPLGLWNRPE
VAELNPSFHN LTQEDMEETF NVGSFAIGKD TMKLKDIYQS LQKIYCGSVG AEYMHITDTE
QKRWIQQRLE PVVGTPVFSK EEKRTFLEEL TAAEGLERYL GAKFPGAKRF SLEGGDALVP
MTKEMIRHAG ASGMREVVIG MAHRGRLNML VNVLGKKPQD LFDEFAGKHG EGWGTGDVKY
HQGFSADFAT PGGDVHLALA FNPSHLEIVN PVVMGSVRAR QDRLGDEDGS KVLPITIHGD
SAIAGQGVVA ETFNMSQARG FCVGGTVRIV VNNQVGFTTS NPRDTRSTMY CTDIAKMVQA
PIFHVNSDDP EAVAFVTRLA LDYRNEFKRD VVIDLVCYRR HGHNEADEPN ATQPLMYQKI
KKHPTPRKLY ADVLTERGEC DLETATQLVN EYRDALDHGE VVVKEWRPMA MHSVDWSPYL
GHDWHIPWNS EYAMERLQDL GRRVCQYPES HVLHSRVEKI YQDRLSMISG EKMLDWGMAE
TLAYATLLDD GKRIRISGQD SGRGTFFHRH AVLHNQNDAS TYIPLSQIHA GQGPFEVFDS
VLSEEAVLAF EYGYATAEPS GLTLWEAQFG DFANGAQVVI DQFISSGEQK WGRLCGLTML
LPHGYEGQGP EHSSARLERY LQLCAEQNMQ VVVPSTPAQV YHMIRRQVVR PMRRPLVVMS
PKSLLRHPLC VSSMEDLAHG TFQPAIGEID ALNPSQVKRV VFCSGKVYYD LLEQRRANEQ
QDVAIVRIEQ LYPFPLEEVQ AAIANYTNVV DYVWCQEEPQ NQGAWYSSQH NFRAAIPAGA
DLKYAGRPAS ASPAVGYMSV HMKQQKALIE DALTLA
//
