ID   A0A0C5V7H5_9GAMM        Unreviewed;       948 AA.
AC   A0A0C5V7H5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=YC6258_03334 {ECO:0000313|EMBL:AJQ95370.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ95370.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ95370.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ95370.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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; CP007142; AJQ95370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C5V7H5; -.
DR   STRING; 1445510.YC6258_03334; -.
DR   KEGG; gsn:YC6258_03334; -.
DR   PATRIC; fig|1445510.3.peg.3296; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000032266; Chromosome.
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   ECO:0000313|EMBL:AJQ95370.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          601..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   948 AA;  107583 MW;  B85F6E6D01EA3A51 CRC64;
     MQDSIMEQLW GTSHLAGGNS SYLEELYESY LRDPNSVPED WRAEFDKLPR VNPSVHSEVP
     HSPIKDHFLL LSKNQKKLST AVLSPSITTE HERKQVRVHQ LATAYRFRGH QKAKLDPLGL
     EQRPSIPDLE LQYHELSKAD EDTVFSCSHL YAGKEEATLK ETIELLEQTY CSSVGAEFTH
     IVDTAERRWI EQRMESVKSH PVYSNEARLH ILERLSAGEG LEKYLQSKYP GTKRFGLEGG
     EALIPLVDEL IQRAGSYGTK EIVLGMAHRG RLNILVNILG KSPRDLFDEF EGKSFYEMGS
     GDVKYHQGFS SNVMTQGGEV HLAMAFNPSH LEIVSPVVEG SVRARQDRRK DPVGTTVLPV
     AIHGDAAFAG QGVVMETFQM SQTRGYKTGG TIHIIVNNQV GFTTSRREDA RSTEYCTDIA
     KMVQAPIFHV NGDDPEAVVF VTQLAVDYRQ QFKRDVVIDM VCYRRRGHNE ADEPAMTQPL
     MYEKIRKIKS TLDLYGERLV NEGVIDKDGV TQMAEEYRTA LENGEHVAKS LVKEPNTSLF
     VDWKPYLNQP FSDDFDTSLD LQYLRELANR INTVPEGFPV QRQVNKIIED RLKMAAGAMP
     INWGFAETLA YATILDSDHP IRITGQDVGR GTFVHRHAVL HSTKDGSTYV PLRNLSEDQP
     EFDIYDSFLS EEAVLAFEYG YATTTPNALV IWEAQFGDFA NGAQVVIDQF ITSGEHKWGR
     LCGLVMLLPH GYEGQGPEHS SARLERYLQL CAEQNIQVCV PSTPAQVYHM LRRQITRNLR
     KPLVVMSPKS LLRHKDAVST LDELATGKFE TVLDDPDITD KDAVQRVVFC SGKVYYDLRE
     RCRRDEIVNV ALVRVEQLYP FPEDRLYQIL STYPKVEDVV WCQEEPMNQG AWYSSQHHLR
     NVIHRHDPDL YLVYVGREAS AAPAAGYMKL HLEQLNKFLE DALVYPKK
//