ID   S7U691_DESML            Unreviewed;       927 AA.
AC   S7U691;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=dsmv_3773 {ECO:0000313|EMBL:EPR44847.1};
OS   Desulfococcus multivorans DSM 2059.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfococcaceae; Desulfococcus.
OX   NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR44847.1, ECO:0000313|Proteomes:UP000014977};
RN   [1] {ECO:0000313|EMBL:EPR44847.1, ECO:0000313|Proteomes:UP000014977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR44847.1,
RC   ECO:0000313|Proteomes:UP000014977};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT   bacteria.";
RL   Genome Announc. 1:e00618-e00613(2013).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EPR44847.1}.
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; ATHJ01000015; EPR44847.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7U691; -.
DR   STRING; 897.B2D07_10460; -.
DR   PATRIC; fig|1121405.3.peg.260; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000014977; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          583..776
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   927 AA;  104850 MW;  D2D5865C3B5398D0 CRC64;
     MIDISETMNM AYIDRQYQLW KNDPDAVERD WRIFFKGFET AGGLDLKTVV RADEGLSRPD
     TDLPEEACTI DKTLLQSRVE ALKYRYRDMG HLLACLDPLV ACPTDHPLLN ISAVGLSPED
     LDTAFYTRRF SKTLTAPLKD IIRELRETYC RSVGVEYMHL QDPEERRWLQ DRMEPIRNQP
     VFSAEDKRRI ITKLYQSAFF ESFLHKKYTG QTRFSLEGAD ALIAAMDALF LHASEQGVTE
     IILGMAHRGR LNVLTNILGK HYEEIFREFI NSYDPESLMG AGDVKYHNGF LADLTLANQR
     KVRAFLVNNP SHLESVDPVV EGIAYARQDA LTPAPRNQVL PLLIHGDSAF AGQGVVAETL
     NLSQLEGYRT EGTVHIIINN QIGYTTLPEN ARSTRYSTDI AKMLMVPIFH VHGENPEAVI
     HVIKLAFDYR MAFGKDVIVD MVCYRRFGHN EGDEPYFTQP AMYERIRERP PLYKIYGEKM
     VDDGEIDDSG LAEIENGLVT CLEEGFSAAQ DNPRIFPVPR FYENWSDYHG DYSFAPVDTA
     VSQKSLKALA AAVNTPPSGF AVHPKLERLL GKRLESVESG RDIDWANAES LAFASLLSEG
     HHVRLSGQDS ARGTFSQRHS ILVDVKTGEF HVPLTGVCRK KAVFSVFNSA LSEAGVLGFE
     YGYSMIRPAG LTLWEAQFGD FVNNAQGIVD LYIVSGETKW QRRSGLVMLL PHGWEGLGPE
     HSSARMERFL QLCAHDNIQV CNPTTPAQYF HLLRRQAKSS WRKPLVLMTP KSLLRHPRAV
     SRIDDFSRGT FQEVIDDDAA VEKARRVIFC SGKIYYQLLE RRETLKAYDI AIVRVEQFYP
     FPREKLERIV GKYRKADQWC WVQEGPVNME GWSFMAPRLK EIVGTDPTYI GRPASASPAT
     GFANIYKQEQ SLLPDKAVGQ LSGVQTG
//