ID W6QXN9_PSEP5 Unreviewed; 943 AA.
AC W6QXN9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:CDM40748.1};
GN ORFNames=BN5_2177 {ECO:0000313|EMBL:CDM40748.1};
OS Pseudomonas pseudoalcaligenes (strain CECT 5344).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=1182590 {ECO:0000313|EMBL:CDM40748.1, ECO:0000313|Proteomes:UP000032841};
RN [1] {ECO:0000313|EMBL:CDM40748.1, ECO:0000313|Proteomes:UP000032841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5344 {ECO:0000313|Proteomes:UP000032841};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of the cyanide-degrading bacterium Pseudomonas
RT pseudoalcaligenes CECT 5344.";
RL Submitted (NOV-2013) 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; HG916826; CDM40748.1; -; Genomic_DNA.
DR RefSeq; WP_003459987.1; NZ_HG916826.1.
DR AlphaFoldDB; W6QXN9; -.
DR GeneID; 61799877; -.
DR KEGG; ppse:BN5_2177; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000032841; 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 ECO:0000313|EMBL:CDM40748.1};
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; 105835 MW; 4DB10AB3B7E65760 CRC64;
MQESVMQRMW DSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPT DGSAAADVPH
STIRDYFVLL AKNSRRAQPV SAGAVSSEHE KKQVEVLRLI QAYRVRGHQA AQLDPLGLWV
RTAPSDLSIN HYGLTDADLD TTFRTGELYI GKEEATLREI LGALQQTYCR TIGAEFMHIV
DSGQRHWFAQ RLESVRGRPQ FSAEVQAHVL ERITAAEGLE KYLGTKYPGT KRFGLEGGES
LIPLLDEIIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRDLFDEFEG KKIEGLSSGD
VKYHQGFSSN VMTAGGEVHL ALAFNPSHLE IVSPVVEGSV RARQDRRNDA SGDKVLPISI
HGDAAFAGQG VVMETFQMSQ TRGYKTGGTI HIVINNQVGF TTSHPEDSRS TEYATDVAKM
IQAPIFHVNG DDPEAVLFVT QLAVDYRMQY KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
QQIAKQRTTR ELYADALVAA GVLSSEDVQA KIDEYRTALD NGQHVVKSLV KEPNKELFVD
WRPYLGHTWT ARHDTRFDLK TLQDLSAKLL EIPEGFLVQR QVAKILEDRQ KMGAGGLPIN
WGFAETMAYA TLLVEGHPIR MTGQDIGRGT FSHRHAVLHN QKDGSTYVPL KNLYDGQPKF
ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EAQFGDFANG AQVVFDQFIS SGETKWGRLC
GLTVLLPHGY EGQGPEHSSA RLERYLQLCA EHNMQVCVPT TPAQVYHMLR RQVIRPLRKP
LVVLTPKSLL RHKLAISTLE DLAEGSFHTV IGEIDSLDPK KVERLILCSG KVYYDLLEKR
RAEGREDIAI IRIEQLYPFP EDDLAEALAP YKNLKHIVWC QEEPMNQGAW YCSQHHMRRV
ATAHKKSLLL EYAGRDASAA PACGYASMHA EQQEKLLQDA FTV
//
