ID   Q7MMN5_VIBVY            Unreviewed;       941 AA.
AC   Q7MMN5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=VV1032 {ECO:0000313|EMBL:BAC93796.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC93796.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC93796.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC93796.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA   Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA   Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(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:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000037; BAC93796.1; -; Genomic_DNA.
DR   RefSeq; WP_011149792.1; NC_005139.1.
DR   AlphaFoldDB; Q7MMN5; -.
DR   STRING; 672.VV93_v1c09550; -.
DR   KEGG; vvy:VV1032; -.
DR   PATRIC; fig|196600.6.peg.1029; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000002675; Chromosome I.
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: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   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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..787
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   941 AA;  106008 MW;  B36F7B589608A3DB CRC64;
     MHNGVMKAWL ESSHLAGANA TYVEDLYELY LSDPDLVSEE WKRVFEGLPK PTKEVAEQPH
     SRVRDYFRRL AQETKHYSVQ VSDPDVDAKQ VKVLQLINAY RFRGHEAAEL DPLGLWQRPT
     VAELDPAFHN LTEDDFEETF NVGSFAVGQE TMPLKDIYTA LKKTYCGSIG AEYMHMTDTE
     QKRWIQQRLE SVVGQPSFDK DEKRTFLAEL TAAEGLERYL GAKFPGAKRF SLEGGDAMIP
     MMKELIRHAG RSGMREVVIG MAHRGRLNML VNVLGKKPQD LFDEFAGKHG ESWGTGDVKY
     HQGFSADFAT PGGDVHLALA FNPSHLEIVN PVVMGSVRAR QDRLGDDDGS KVLPITIHGD
     SAIAGQGVVA ETFNMSQARG FCVGGTVRVV VNNQVGFTTS NPRDTRSTMY CTDIAKMVQA
     PIFHVNADDP EAVAFVTRIA LDYRNEFKRD VVIDLVCYRR HGHNEADEPN ATQPLMYQKI
     KKHPTPRKLY ADVLIDRNEC DIETATQMVN EYRDALDHGE VVVKEWRPMA LHSVDWSPYL
     GHDWDTPWSN TYDKQRLVEL GKRLCQYPES HTLHSRVSKL YNDRTAMTNG EKELDWGMAE
     TLAYATLVDD GKRIRISGQD SGRGTFFHRH AVLHNQNDAS TYVPLANIHD KQGPFEVFDS
     VLSEEAVLAF EYGYATAEPS GLTLWEAQFG DFANGAQVVI DQFISSGEQK WARLCGLTML
     LPHGYEGQGP EHSSARLERY LQLCAEQNMQ VVVPSTPAQV YHMIRRQVVR PMRRPLIVMS
     PKSLLRHPLC TSSLDDLANG TFMPAIPEID ELDPAKVKRV VFCSGKVYFD LLEQRRNNEQ
     DDVAIVRIEQ LYPFPMDDVK AAIAPYVNVE DFVWCQEEPQ NQGAWYCSQH NFRAAIPAGT
     ELKYAGRPAS ASPAVGYMSV HLKQQKALID DALNVNEKTS D
//