ID   A0A1H1B8X6_9BURK        Unreviewed;       953 AA.
AC   A0A1H1B8X6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05443245_1554 {ECO:0000313|EMBL:SDQ48387.1};
OS   Paraburkholderia fungorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=134537 {ECO:0000313|EMBL:SDQ48387.1, ECO:0000313|Proteomes:UP000183487};
RN   [1] {ECO:0000313|Proteomes:UP000183487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA   Varghese N.;
RL   Submitted (OCT-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; FNKP01000001; SDQ48387.1; -; Genomic_DNA.
DR   RefSeq; WP_074763755.1; NZ_FNKP01000001.1.
DR   AlphaFoldDB; A0A1H1B8X6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000183487; 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          599..796
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   953 AA;  106580 MW;  8E868CDBA02C4386 CRC64;
     MMKQFQSNSY LFGGNAPYVE EMYEAYLDNP ASVPENWRSY FDALQNVPAT DGTNANDVAH
     GPIVESFAQR AKANAFIPRT AAGGEDLATA RKQVYVQSLI GAYRFLGSQW ANLDPLKRRE
     RPAIPELEPA FYDFTEADMD QEFSATNLYF GFEKASLREI VKALRDTYCG QIGAEYMYIS
     DPEQKRWWKE RLESIRSTPN FSNDKKKHIL NRLTAAEGLE RFLHTKYVGQ KRFSLEGGES
     FIASMDEVVR HGGAKGVQEI VIAMAHRGRL NVLVNTLGKM PADLFAEFEG KHVDDLPAGD
     VKYHKGFSSD VATDGGPVHL SLAFNPSHLE IVNPVVEGSA KARMDRRGDD SGLQVLPVQI
     HGDAAFAGQG VVMETLNLAQ TRGYGTHGTL HIVINNQIGF TTSDPRDSRS TLYCSDVVKM
     IEAPVLHVNG DDPEAVVLAT QMAIDFRMQF HKDVVVDIVC FRKLGHNEQD TPAVTQPLMY
     KTIAKHPGTR ALYAEKLVQQ GVITAEEGDD FVKAYRKAMD EGHHTVDPVL SNYKSKYAVD
     WVPFLNRKWT DAADTAVPLA ELKRLAERIT TVPENFKVHP LVERVLNDRR AMGRGEAKLD
     WGMGEHLAFA SLVASGYAVR LTGQDSGRGT FTHRHAVLHD QNRERWNDGT YVPLQNVSEG
     QAKFNVIDSV LSEEAVLGFE YGYSTAEPNT FVAWEAQFGD FVNGAQVVID QFISSGEVKW
     GRVSGLTMLL PHGYEGQGPE HSSARIERFL QLCADHNMQV VQPTTPAQIF HLLRRQMIRL
     FRKPLIVATP KSLLRHKEAV SDLSELAKGA FQPILGEVDE AIDAKKVKRL VVCSGRVYYD
     LVAHRRETKA NDVAIIRIEQ LYPFAHKQFE AEIKKYDNAT EVVWVQDEPQ NQGPWFYIEH
     HLKDGMKEGQ KLAYSGRPAS ASPAVGYYAK HYEQQKALIE GAFGRLKSAS IAK
//