ID A0A2P8KH72_9BURK Unreviewed; 959 AA.
AC A0A2P8KH72;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:PSL82285.1};
GN ORFNames=C7T35_22510 {ECO:0000313|EMBL:PSL82285.1}, GXN78_02885
GN {ECO:0000313|EMBL:NDZ11826.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL82285.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL82285.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL82285.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ11826.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ11826.1,
RC ECO:0000313|Proteomes:UP000479786};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) 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:PSL82285.1}.
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DR EMBL; JAAGOW010000001; NDZ11826.1; -; Genomic_DNA.
DR EMBL; PXZZ01000032; PSL82285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KH72; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; 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:PSL82285.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 606..803
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 959 AA; 106368 MW; EC687938CD42AE6B CRC64;
MSDSTSSASI YHAYQGNTYL FGGNAPYVEE MYENYLANPG SVPDNWRSYF DALQNVPATD
GSTTRDVPHQ PVINAFAERA KQGTTKVVQA SGADSELGRQ RTAVQQLIAA YRNVGARWAD
LDPLKRAERP PIPELEPSFY GFTDADLETV FNTSNTFFGK DTMSLRDLLN ALRETYCTTI
GAEYMYMTDQ AQKRWWQQKL ESARTNPKLS TEQKKRILER LTAAEGLERF LHTKYVGQKR
FSLEGGESFI VSMDELISQA GTKGVQEIVI GMAHRGRLNV LVNSLGKMPA DLFAEFDHTA
PEELPSGDVK YHQGFSSDVS TPGGPVHLSL AFNPSHLEIV NPVVEGSVRA RMDRRADPLG
KQVLPVIVHG DAAFAGQGVV METLALAETR GYSTGGTVHI VINNQIGFTT SDPRDSRSTL
YCTDIVKMNE APVLHVNGDD PEAVVLATQL ALEFRMEFQK DVVVDIVCFR KLGHNEQDTP
SLTQPLMYKK IAAHPGTRRL YADRLAAQGL GETLGDDLVK AQRAAFDAGK NTTNPVLTNF
KSKYAVDWSP FLNKKWTDAG DTAIPTAEWK RLAERITKAP DNFTVHPLVK KVLDDRAAMG
RGEINVDWGM GEHMAFASLV ASGYPVRLSG EDSGRGTFTH RHAVLHDQNR EKFDVGTYVP
LQNVADNQAP FVVIDSILSE EAVLAFEYGY ASNDPNTLVI WEAQFGDFAN GAQVVIDQFI
ASGEVKWGRV NGITLMLPHG YEGQGPEHSS ARLERFMQLS ADANMQVVQP TTASQIFHVL
RRQMVRNLRK PLVIMTPKSL LRNKDATSPL SEFTKGSFQT VIPDNKELKA DKVKRVIACS
GKVYYDLAKK REEKGSEDVA IIRVEQLYPF PHKAFATELK KYPNLVDVVW SQDEPQNQGA
WFFVQHNIHE NLQEGQKLGY SGRAASASPA VGYSHLHQEQ QKALVDGAFA KLKGFVLTK
//
