ID   I7B4Q2_PSEPT            Unreviewed;       943 AA.
AC   I7B4Q2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=T1E_0429 {ECO:0000313|EMBL:AFO46288.1};
OS   Pseudomonas putida (strain DOT-T1E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1196325 {ECO:0000313|EMBL:AFO46288.1, ECO:0000313|Proteomes:UP000006503};
RN   [1] {ECO:0000313|Proteomes:UP000006503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOT-T1E {ECO:0000313|Proteomes:UP000006503};
RX   PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA   Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA   Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT   "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT   DOT-T1E deduced from its annotated genome.";
RL   Microb. Biotechnol. 6:598-611(2013).
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; CP003734; AFO46288.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7B4Q2; -.
DR   KEGG; ppx:T1E_0429; -.
DR   PATRIC; fig|1196325.3.peg.432; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000006503; 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   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;  106520 MW;  FA5B2678C2724E9C CRC64;
     MQESVMQRMW DSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSTATDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AKLDPLGLWQ
     RPAPVDLSIN HYGLTNADLD TTFRAGDLFI GKEEASLRDI FDALQKTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPE FSADVQAHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDEMIQ RSGSYGAKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKMNELGSGD
     VKYHQGFSSN VMTPGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDT VGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDARS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLAIDYRMQF KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQISKQRTTR ELYAEQLIQA GRIDAERAQA KIDEYRNALD NGLHVVKSLV KEPNRELFVD
     WRPYLGHAWT ARHDTRFDLK TLQDLSAKLL ELPEGFVVQR QVSKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLQFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDASTYIPL KNLFPGQPRF
     DLYDSFLSEE AVLAFEYGYS TTMPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LVVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEIDAIDPA KVERLVLCSG KVYYDLLEKR
     RAEGREDIAI LRIEQLYPFP EDDLVEILAP YTNLKHAVWC QEEPMNQGAW YSSQHHMRRI
     LGRHNKALVL EYAGRDASAA PACGYASKHA EQQEKLLQDA FTV
//