ID   A0A1G6L951_9BURK        Unreviewed;       954 AA.
AC   A0A1G6L951;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05421548_106152 {ECO:0000313|EMBL:SDC39607.1};
OS   Paraburkholderia lycopersici.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=416944 {ECO:0000313|EMBL:SDC39607.1, ECO:0000313|Proteomes:UP000198908};
RN   [1] {ECO:0000313|Proteomes:UP000198908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2016) 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; FMYQ01000006; SDC39607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6L951; -.
DR   STRING; 416944.SAMN05421548_106152; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000198908; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          600..797
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   954 AA;  106838 MW;  7B8DA39AE7FB1C63 CRC64;
     MSETMKQFQL NSYLFGGNAP YVEELYEAYL DNPASVPDAW REYFDALQNV PSSSGTADND
     IAHGPIVESF AQRAKANAFV ARGGGEDLAT ARKQVYVQSL IGAYRFLGSQ WANLDPLKRR
     ERPNIPELEP AFYDFTEADM DQTFSATNLY FGFERATLRE IVKALRDTYC GTIGAEYMYI
     SDPEQKRWWK ERLESIRSTP NFTTDKKKHI LQRLTAAEGL ERFLHTKYVG QKRFSLEGGE
     SFIAAMDEVV RHAGAKGVQE IVIGMAHRGR LNVLVNTLGK MPADLFAEFE GKHVDDLPAG
     DVKYHKGFSS DVATEGGPVH LSLAFNPSHL EIVNPVVEGS AKARMDRRGD DNGLQVLPVQ
     IHGDAAFAGQ GVVMETLNLA QTRGYGTHGT LHIVINNQIG FTTSDPRDAR STLYCTDVVK
     MIEAPVLHVN GDDPEAVVLA IQFAVDFRMQ FHKDVVVDIV CFRKLGHNEQ DTPAVTQPLM
     YKKIAQHPGT RALYAEKLVQ QGVITAEDGD SYVKAYRAAM DEGHHTVDPV LSNYKSKYAV
     DWVPFLNRKW TDAADTAVPL AELKRLAERI TTIPENFKVH PLVERVINDR RAMGKGEHKL
     DWGMGEHLAF ASLVASGYAV RLTGQDSGRG TFTHRHAVLH DQNRERWNDG TYVPLQNISE
     NQAKFTVIDS VLSEEAVLGF EYGYSTAEPN TFVAWEGQFG DFVNGAQVVI DQFISSGEVK
     WGRVSGLTML LPHGYEGQGP EHSSARIERF LQLCADHNMQ VVQPTTPAQI FHVLRRQMIR
     LFRKPLIIFT PKSLLRHKEA VSDLSELAKG TFQPVIGEVD ETIDAKKVKR VVACSGRVYF
     DLVAHRREAK ATDVAIIRIE QLYPFAHKQF EAELKKYDNA TEVVWVQDEP QNQGPWFYIE
     HHLKEGMKEG MKLAYSGRPA SASPAVGYYA KHYEQQKALI EGAFGRLKGV QVAK
//