ID   A0A167VWV6_9BURK        Unreviewed;       953 AA.
AC   A0A167VWV6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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   Name=sucA {ECO:0000313|EMBL:ANB72323.1};
GN   ORFNames=AYM40_08080 {ECO:0000313|EMBL:ANB72323.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB72323.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB72323.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB72323.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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; CP014578; ANB72323.1; -; Genomic_DNA.
DR   RefSeq; WP_063495760.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A167VWV6; -.
DR   STRING; 1804984.AYM40_08080; -.
DR   KEGG; buz:AYM40_08080; -.
DR   Proteomes; UP000076852; Chromosome 1.
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:UP000076852};
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;  106498 MW;  64C9CC0B4CA6808F CRC64;
     MMKQFQSNSY LFGGNAPYVE EMYEAYLDNP ASVPENWRSY FDALQNVPAS DGSNANDVAH
     GPIVESFAQR AKANAFIPRT AAGGEDLATS RKQVYVQSLI GAYRFLGSQW ANLDPLKRRE
     RPAIPELEPA FYDFTEADMD QEFSATNLYF GFERASLREI VKALRDTYCG TIGAEYMYIS
     DPEQKRWWKE KLESIRSTPS FSNEKKKHIL NRLTAAEGLE RFLHTKYVGQ KRFSLEGGES
     FIASMDEVVR HGGANGVQEI VIGMAHRGRL NVLVNTLGKM PADLFAEFEG KHVDDLPAGD
     VKYHKGFSSD VSTDGGPVHL SLAFNPSHLE IVNPVVEGSA KARMDRRGDD SGLQVLPVQI
     HGDAAFAGQG VVMETLNLAQ TRGYGTHGTL HIVINNQIGF TTSDPRDSRS TLYCSDVVKM
     IEAPVLHVNG DDPEAVVLAT QLAIDFRMQF HKDVVVDIVC FRKLGHNEQD TPAVTQPLMY
     KTIAKHPGTR ALYAEKLVQQ GVITAAEGDE FVKAYRKAMD EGHHTIDPVL SNYKSKYAVD
     WVPFLNRKWT DAADTAVPLA ELKRLAERVT TIPENFKVHP LVERVINDRR AMGRGEAKLD
     WGMGEHLAFA SLVASGYAVR LTGQDSGRGT FTHRHAVLHD QNRERWNDGT YVPLQNIAEG
     QAKFTVIDSV LSEEAVLGFE YGYSTAEPNT FVAWEAQFGD FVNGAQVVID QFISSGEVKW
     GRVSGLTMLL PHGYEGQGPE HSSARIERFL QLCADHNMQV VQPTTPAQIF HLLRRQMIRL
     FRKPLIVATP KSLLRHKEAV SDLSELAKGA FQPILGEIDE AIEPKKVKRV VACSGRVYYD
     LLAHRRESKS NDVAIIRIEQ LYPFAHKQFE AEMKKYDNAT EVVWVQDEPQ NQGPWFYIEH
     HLKEGMKDGQ KLAYSGRPAS ASPAVGYYAK HYEQQKALIE GAFGRLKSAS IAK
//