ID   A0A0F7Y3B4_9PSED        Unreviewed;       943 AA.
AC   A0A0F7Y3B4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:CRI56153.1};
GN   ORFNames=CCOS191_1617 {ECO:0000313|EMBL:CRI56153.1};
OS   Pseudomonas sp. CCOS 191.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1649877 {ECO:0000313|EMBL:CRI56153.1, ECO:0000313|Proteomes:UP000033942};
RN   [1] {ECO:0000313|Proteomes:UP000033942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCOS 191 {ECO:0000313|Proteomes:UP000033942};
RA   Blom J.;
RL   Submitted (APR-2015) 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; LN847264; CRI56153.1; -; Genomic_DNA.
DR   RefSeq; WP_046854765.1; NZ_LN847264.1.
DR   AlphaFoldDB; A0A0F7Y3B4; -.
DR   KEGG; psec:CCOS191_1617; -.
DR   PATRIC; fig|1649877.3.peg.1646; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000033942; Chromosome I.
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:CRI56153.1};
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;  106356 MW;  260BED48396016E4 CRC64;
     MQESVMQRMW ESAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFQKLPA DGSTATDVSH
     STIRDHFVLL AKNQRRAQPV SAGSVSSEHE KKQVEVLRLI QAYRMRGHQA AKLDPLGLWQ
     RPAPVDLSIN HYGLTNADLD TTFRAGDLFI GKEEASLREI SEALQKTYCR TIGAEFTHIV
     DSEQRSWFQQ RLESVRGRPE FSADVQAHLL ERVTAGEGLE KYLGTKYPGT KRFGLEGGES
     LIPMLDEMIQ RSGSYGTKEV VIGMAHRGRL NVLVNTFGKN PRELFDEFEG KKMNELGSGD
     VKYHQGFSSN VMTAGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRNDT VGDKVLPISI
     HGDAAFAGQG VVMETFQMSQ TRGFKTGGTV HIVINNQVGF TISNPLDSRS TEYATDVAKM
     IQAPILHVNG DDPEAVLFVT QLAIDYRMQF KRDVVIDLVC YRRRGHNEAD EPNGTQPLMY
     QQISKQRTTR ELYADALIQA GRIDAERAQA KIDDYRNALD NGLHVVKSLV KEPNRELFVD
     WRPYLGHAWT ARHDTRFDLK TLQELSAKLL ELPEGFVVQR QVSKIYEDRQ KMQAGGLPIN
     WGYAETMAYA TLQFEGHPIR MTGQDIGRGT FSHRHAVLHN QKDASTYVPL QNLFPGQPRF
     DLYDSFLSEE AVLAFEYGYS TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQIYHLLR RQVIRPLRKP
     LVVLTPKSLL RHKLAISTLE DLAEGSFQTV IPEIDTLDPA KVERIVLCSG KVYYDLLEKR
     RAEGREDIAI VRIEQLYPFP EDDLVEILAP YTNLKAAVWC QEEPMNQGAW YSSQHHMRRI
     LGRHNKALVL EYAGRDASAA PACGYASKHA EQQEKLLQDA FTV
//