ID   C0PWE5_SALPC            Unreviewed;       933 AA.
AC   C0PWE5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:ACN44908.1};
GN   OrderedLocusNames=SPC_0733 {ECO:0000313|EMBL:ACN44908.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN44908.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN44908.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN44908.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN44908.1; -; Genomic_DNA.
DR   RefSeq; WP_001181504.1; NC_012125.1.
DR   AlphaFoldDB; C0PWE5; -.
DR   KEGG; sei:SPC_0733; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000001599; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          591..784
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   933 AA;  104852 MW;  FFA03552C40A3F24 CRC64;
     MQNSALKAWL DSSYLSGSNQ SWIEQLYEDF LTDPDSVDAN WRLTFQQLPG TGVKPDQLHS
     KTREYFRRQA LAGSRHSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWKQERV
     ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLDAL KQTYCGPIGA EYMHITSTEE
     KRWIQQRIES GRAAFSADEK KRFLNELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK
     EMVRHAGNSG TREVVLGMAH RGRLNVLINV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG
     FSSDIETEGG LVHLALAFNP SHLEIVSPVV MGSVRARLDR LDEPSSNKVL PITIHGDAAV
     TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF
     HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH
     PTPRKIYADK LEADKVATLE DATEMVNLYR DALDAGECVV KEWRPMNMHS FTWSPYLNHE
     WDESYPNKVE MKRLQELAKR ISTVPEAIEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA
     YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQTNGSTYT PLQHIHSGQG QFKVWDSVLS
     EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH
     GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS
     LLRHPLAVST LDELANGSFQ PAIGEIDELD PKAVKRVVMC SGKVYYDLLE QRRKNDQKDV
     AIVRIEQLYP FPHKAVQEAL QPYAHVHDFV WCQEEPLNQG AWYCSQHHFR EVIPFGAALR
     YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVD
//