ID   B1JAV6_PSEPW            Unreviewed;       943 AA.
AC   B1JAV6;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=PputW619_3512 {ECO:0000313|EMBL:ACA73995.1};
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA73995.1};
RN   [1] {ECO:0000313|EMBL:ACA73995.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W619 {ECO:0000313|EMBL:ACA73995.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Psuedomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA73995.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1JAV6; -.
DR   STRING; 390235.PputW619_3512; -.
DR   KEGG; ppw:PputW619_3512; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
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:ACA73995.1};
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;  106408 MW;  E9BC015E56D970D8 CRC64;
     MQESVMQRMW ESAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSTATDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AKLDPLGLWQ
     RPAPVDLSIN HYGLTNADLD TTFRAGDLYI GKEEASLREI VEALQKTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPD FSADVQAHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDEMIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKMNELGSGD
     VKYHQGFSSN VMTTGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDT AGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDSRS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLAIDYRMQF KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQISKQRTTR ELYAEALIQA GRIDAERAQA KIDEYRNALD NGLHVVKSLV KEPNRELFVD
     WRPYLGHAWT ARHDTRFDLK TLQDLSAKLL ELPEGFVVQR QVSKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLQFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDASTYVPL QNLFPGQPRF
     DLYDSFLSEE AVLAFEYGYS TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LIVLTPKSLL RHKLAVSTLE DLAEGSFQTV IPEIDTLDPA KVERLVLCGG KVYYDLLEKR
     RAEGREDIAI VRIEQLYPFP EDDLVDILAP YTNLKHAVWC QEEPMNQGAW YSSQHHMRRI
     LGRHNKALVL EYAGRDASAA PACGYASKHA EQQEKLLQDA FTV
//