ID D2TPD0_CITRI Unreviewed; 935 AA.
AC D2TPD0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:CBG87499.1};
GN OrderedLocusNames=ROD_07231 {ECO:0000313|EMBL:CBG87499.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG87499.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG87499.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG87499.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG87499.1; -; Genomic_DNA.
DR RefSeq; WP_012905051.1; NC_013716.1.
DR AlphaFoldDB; D2TPD0; -.
DR STRING; 637910.ROD_07231; -.
DR KEGG; cro:ROD_07231; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001889; 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:CBG87499.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 593..786
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 104953 MW; A80D299CD59462E8 CRC64;
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQLHS
KTREYFRRLA KDASRYSSSI SDPDANVKQV KVLQLINAYR FRGHQHANLD PLGLWKQDTV
ADLDPSFHDL TEADFQETFN VGSFAIGKDT MKLGDLIDAL RQTYCGSIGA EYMHITSTEE
KRWIQQRIES VAGHATFSVE EKKRFLGELT AAEGLERYLG AKFPGAKRFS LEGGDALIPM
LKEMIRHAGS SGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFAGKHKE HLGTGDVKYH
MGFSSDIETE GGLVHLALAF NPSHLEIVSP VVMGSVRARL DRLDEPSSNK VLPITIHGDA
AVTGQGVVQE TLNMSKARGY EVGGTVRIVI NNQVGFTTSN PLDARSTPYC TDIGKMVQAP
IFHVNADDPE AVAFVTRLAL DFRNTFKRDV FIDLVCYRRH GHNEADEPSA TQPLMYQKIK
KHPTPRKIYA DKLEADKVAT LEDATEMVNL YRDALDAGEC VVKEWRPMNM HSFTWSPYLN
HDWEEAYPNK VEMKRLQELA KRISTVPEAV EMQSRVAKIY GDRQAMAAGE KLFDWGGAEN
LAYATLVDEG IPVRLSGEDS GRGTFFHRHA VIHNQSNGST YTPLQHVHNG QGTFRVWDSV
LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLVVMSP
KSLLRHPLAV SSLNELANGA FLPAIGEIDD IDPKGVKRVV MCSGKVYYDL LEQRRKNDQK
DVAIIRIEQL YPFPHQAMQD VLKQYAHVHD FVWCQEEPLN QGAWYCSQHH FREVIPFGSA
LRYAGRPASA SPAVGYMSVH QKQQQDLVND ALNVD
//
