ID   O85487_PSEPU            Unreviewed;       943 AA.
AC   O85487;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=kgdA {ECO:0000313|EMBL:AAC23516.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303 {ECO:0000313|EMBL:AAC23516.1};
RN   [1] {ECO:0000313|EMBL:AAC23516.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PpG2 {ECO:0000313|EMBL:AAC23516.1};
RA   Madhusudhan K.T., Clifton S., Roe B.A.;
RT   "Nucleotide sequence of genes encoding alpha-ketoglutarate dehydrogenase
RT   and dihydrolipoamide succinyltransferase components of Pseudomonas putida
RT   PpG2.";
RL   Submitted (MAY-1998) 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; AF068740; AAC23516.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85487; -.
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;  106528 MW;  02B54AA5D0942F7B CRC64;
     MQDSVMQRMW ESAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSTATDVSH
     STIRDQFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AKLDPLGLWQ
     RPAPVDLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI FEALQKTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPE FSADVQAHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDEMIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKMNELGSGD
     VKYHQGFSSN VMTAGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDT VGDKVLPISI
     HGDKAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDARS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLRIDYRMQF KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQISKQRTTR ELYAEALIQA GRIDAERAQA KIDEYRNALD NGLHVVKSLV KEPNRELFVD
     WRPYLGHAWT ARHDTRFDLK TLQDLSAKLL EIPEGFVVQR QVAKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLQFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDASTYVPL KNLFPGQPMF
     ELYDSFLSEE AVLAFEYGYS TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAHIYHLLR RQVIRPLRKP
     LIVLTPKSLL RHKLAVSTLE DLAEGSFQTV IPEIDTLDPA KVERLVLCGG KVYYDLLEKR
     RAEGREDIAI VRIEQLYPFP EDDLVEILAP YTNLKHAVWC QEEPMNQGAW YSSQHHMRRI
     LGRLNKALVL EYAGRDASAA PACGYASKHA EQQEKLLQDA FTV
//