ID   A0A4U8V487_9BURK        Unreviewed;       950 AA.
AC   A0A4U8V487;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=MW7_012565 {ECO:0000313|EMBL:TMS57431.1};
OS   Burkholderiaceae bacterium PBA.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae.
OX   NCBI_TaxID=795666 {ECO:0000313|EMBL:TMS57431.1, ECO:0000313|Proteomes:UP000004277};
RN   [1] {ECO:0000313|EMBL:TMS57431.1, ECO:0000313|Proteomes:UP000004277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBA {ECO:0000313|EMBL:TMS57431.1,
RC   ECO:0000313|Proteomes:UP000004277};
RA   Gan H.M.;
RT   "Revised genome assembly of Burkholderiaceae (previously Ralstonia) sp.
RT   PBA.";
RL   Submitted (MAY-2019) 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};
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:TMS57431.1}.
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DR   EMBL; AKCV02000023; TMS57431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U8V487; -.
DR   STRING; 795666.MW7_3491; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000004277; 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   ECO:0000313|EMBL:TMS57431.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004277};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          597..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   950 AA;  105771 MW;  3265059F795037C0 CRC64;
     MMQQYKSNSY LFGGNAPYVE ELYEAYLDNP TSVPDNWRAY FDAMQNVPAV DGSDARDVPH
     APIIASFAER AKQGPIRTIV ASADAEMGRK RVAVTQLIAA YRNIGLRWAD LDPLKRQERP
     DVPDLDPAFY GFSDADLDIV FNTNNTYFGK DSMSLRELLT NLRETYSSNI GAEFMYISDQ
     TQKRWWQERL ESSRTKPVFS TEKKKHILER LTAAEGLERF LHTKYVGQKR FSLEGGESFI
     AAMDELIQHG GVKGVQEIII GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK
     YHKGFSSDVS TAGGPVHLSL AFNPSHLEIV NPVVEGSVKA RQERRGDVQG TQVLPVLVHG
     DAAFAGQGVV METLNLAQTR GYGTGGTVHI VINNQIGFTT SDPRDSRSTL YCSDVVKMIE
     APVLHVNGDD PEAVVFAMQL AVDYRTEFRQ DVVVDIICYR KLGHNEQDTP AVTQPLMYKK
     IAAHPGTRKL YADKLAAQGV VDAAYGDELA QAFRSALDAG KHTVDPVLSN YKNKFSVDWL
     PFLNKKWTDA ADTSVPVTEL KRLAERITTI PEDLKVHPLV ERVIKDRAAM GRGELPLDWG
     MGEHLAFASL VASGYPVRIT GQDAGRGTFT HRHAVLHDQK RERWDAGTYV PLQNVSENQA
     PFTVIDSVLS EEAVLGFEYG YSTAEPNALV IWEAQFGDFV NGAQVVIDQF ISSGEVKWGR
     ASGLTLMLPH GYEGQGPEHS SGRIERFLQL SADNNMQVVQ PTTPAQIFHL LRRQMIRMFR
     KPLIIFTPKS LLRNKDATSQ LSELAKGHFE TVIGEQEDIN AAKVKRVIAC SGKVYYDLVN
     ARRERGDNDV AIIRVEQLYP FPHKAAAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYLM
     ENMTEGQKLG YAGRAASASP AVGYYAKHAE QQKQLLDAAF SKLKGFVLTK
//