ID   A7MQX7_CROS8            Unreviewed;       935 AA.
AC   A7MQX7;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=ESA_02622 {ECO:0000313|EMBL:ABU77862.1};
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU77862.1, ECO:0000313|Proteomes:UP000000260};
RN   [1] {ECO:0000313|EMBL:ABU77862.1, ECO:0000313|Proteomes:UP000000260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU77862.1,
RC   ECO:0000313|Proteomes:UP000000260};
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000783; ABU77862.1; -; Genomic_DNA.
DR   RefSeq; WP_007848384.1; NC_009778.1.
DR   AlphaFoldDB; A7MQX7; -.
DR   GeneID; 56731417; -.
DR   KEGG; esa:ESA_02622; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000000260; 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   Reference proteome {ECO:0000313|Proteomes:UP000000260};
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;  104968 MW;  9871B840D8AF827B CRC64;
     MQNGAMKAWL DSSYLSGSNQ SWIEQLYEDF LTDPDSVDAH WRSMFQQLPG TGAKPDQFHS
     KTRDYFRRLA KDASRYSSSI SDPDTNAKQV KVLQLINAYR FRGHQHANLD PLGLWQQERV
     ADLDPAFHDL TEADFQETFN VGSFALGKET MKLGDLIEAL KQTYCGSIGA EYMHITSTEE
     KRWIQQRIES VAGHAGFSAD EKKRFLSELT AAEGLERYLG AKFPGAKRFS LEGGDALIPM
     LKEMIRHAGK SGTREVVLGM AHRGRLNVLI NVLGKKPQDL FDEFAGKHKE HLGTGDVKYH
     MGFSSDIETE GGLVHLALAF NPSHLEIVSP VVMGSVRARL DRLDEPSSNK VLPITIHGDA
     AVAGQGVVQE TLNMSKARGY EVGGTVRIVI NNQVGFTTSN PLDARSTPYC TDIGKMVMAP
     IFHVNADDPE AVAFVTRLAL DFRNTFKRDV FIDLVCYRRH GHNEADEPSA TQPLMYQKIK
     KHPTPRKIYA DKLEQEGVAK LEDATEMVNL YRDALDAGEC VVKEWRPMNM HSFTWSPYLN
     HEWDESYPNK VEMKRLQELA KRISTVPDGI EMQSRVAKIY GDRQLMANGE KPFDWGGAET
     LAYATLVDEG IPVRLSGEDS GRGTFFHRHA VVHNQANGST WVPLQHIHNG QGQFKVWDSV
     LSEEAVLAFE YGYATAEPRT LTIWEAQFGD FANGAQVVID QFISSGEQKW GRMCGLVMLL
     PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLVVMSP
     KSLLRHPLAV SSLEELANGA FLPAIGEVDE LDPQGVKRVV LCSGKVYYDL LEQRRKNDQK
     DVAIVRIEQL YPFPHHAVQE ALKPFAHVHD FVWCQEEPLN QGAWYCSQHH LREVIPFGSA
     LRYAGRPASA SPAVGYMSVH QKQQQDLVND ALNVN
//