ID   A0A1Y0KS88_9PSED        Unreviewed;       943 AA.
AC   A0A1Y0KS88;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=B9K09_12005 {ECO:0000313|EMBL:ARU88644.1};
OS   Pseudomonas sp. M30-35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1981174 {ECO:0000313|EMBL:ARU88644.1, ECO:0000313|Proteomes:UP000196445};
RN   [1] {ECO:0000313|EMBL:ARU88644.1, ECO:0000313|Proteomes:UP000196445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M30-35 {ECO:0000313|EMBL:ARU88644.1,
RC   ECO:0000313|Proteomes:UP000196445};
RA   He A., Zhao Q., Li H., Zhang J.;
RT   "Complete genome sequence of the plant growth-promoting rhizobacterium
RT   Pseudomonas rhizovicinus strain M30-35.";
RL   Submitted (APR-2017) 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; CP020892; ARU88644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0KS88; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000196445; Chromosome.
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:UP000196445};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..792
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   943 AA;  106349 MW;  01834994BA5A369F CRC64;
     MQESVMQRMW DSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGGATTDVSH
     STIRDHFVLL AKNKARAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AQLDPLGLWQ
     RPLPADLSIN HYSLTDADMD TTFRTGGLVI GKEEASLREI LEALQQTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPQ YSAEVQGHVL ERLTAAEGLE KYLGTKYPGT KRFGLEGGES
     LIPLLDEIIQ RSGSYGTKEI VIGMAHRGRL NVLVNTFGKN PRDLFDEFEG KKTEGLSSGD
     VKYHQGFSSN VMTAGGEVHL ALAFNPSHLE IVSPVVEGSV RARQDRRSDN VGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTI HIVINNQVGF TISRVDDARS TEYCTDVAKM
     IQAPIFHVNG DDPEAVLFVT QMAVDYRMQY KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQIAKQRTTR ELYAEMLVNA SRQTAEDVQA KSDEYRAALD NGQHVVKSLV KEPNKELFVD
     WRPYLGHAWT ARHDTRFDLK TLQELSAKLL ETPDGFVVQR QVSKIYEDRQ KMTAGALPIN
     WGYAETMAYA TLLFEGHPIR ITGQDVGRGT FSHRHAVLHN QKDGTPYIPL QKLYDDQPEF
     DLYDSFLSEE AVLAFEYGYS TTTPNGLVIW EAQFGDFANG AQVVFDQFIS SGETKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNMQVCVPT TPAQIYHLLR RQVIRPLRKP
     LVVLTPKSLL RHKLATSTLE DLAEGSFQTV IPEIDPIDPK KVDRVVMCSG KVYYDLLEKR
     RNEGLNNIAI VRLEQLYPFP EDDLTEALAV YKNLKHIVWC QEEPMNQGAW YCSQHHMRRV
     VTAHKKTLVL EYAGREGSAS PACGYASLHA EQQEKLLQDA FTV
//