ID   G8AA97_PSEPU            Unreviewed;       943 AA.
AC   G8AA97;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ADQ74627.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303 {ECO:0000313|EMBL:ADQ74627.1};
RN   [1] {ECO:0000313|EMBL:ADQ74627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RW10S1 {ECO:0000313|EMBL:ADQ74627.1};
RA   Li W., Estrada-de los Santos P., Matthijs S., Xie G.-L., Busson R.,
RA   Cornelis P., Rozenski J., De Mot R.;
RT   "Promysalin, a Salicylate-Containing Pseudomonas putida Antibiotic,
RT   Promotes Surface Colonization and Selectively Targets Other Pseudomonas.";
RL   Chem. Biol. 18:1320-1330(2011).
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; GU211010; ADQ74627.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8AA97; -.
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;  106535 MW;  0AEE71D231DC330D CRC64;
     MQESVMQRMW ESAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSTATDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSTEHE KKQVEVLRLI QAYRMRGHQA AKLDPLGLWQ
     RPAPVDLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI FEALQKTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPE FSADVQAHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDEMIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKMNELGSGD
     VKYHQGFSSN VMTPGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDT LGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDARS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLAVDYRMQF KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQISKQRTTR ELYAESLIQA GRIDAERAQA KIDEYRNALD NGLHVVKSLV KEPNRELFVD
     WRPYLGHAWT ARHDTRFDLK TLQDLSAKLL ELPEGFVVQR QVAKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLQFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDASTYVPL KNLFPGQPRF
     ELYDSFLSEE AVLAFEYGYS TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LIVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEIDTLDPA KVERLVLCGG KVYYDLLEKR
     RAEGREDIAI VRIEQLYPFP EDDLVEILSP YTNLKHAVWC QEEPMNQGAW YSSQHHMRRI
     LGRHNKALVL EYAGRDASAA PACGYASKHA EQQEKLLQDA FTV
//