ID   B7UPL5_ECO27            Unreviewed;       914 AA.
AC   B7UPL5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   18-JUN-2025, entry version 75.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=E2348C_4370 {ECO:0000313|EMBL:CAS11918.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS11918.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS11918.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; FM180568; CAS11918.1; -; Genomic_DNA.
DR   RefSeq; WP_001339449.1; NC_011601.1.
DR   AlphaFoldDB; B7UPL5; -.
DR   KEGG; ecg:E2348C_4370; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
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:TreeGrafter.
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; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008205};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          569..762
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   914 AA;  102266 MW;  74B15DD6695B50B7 CRC64;
     MENMTSPGTL LSGDNATWLE EYYQTWLRTP EKLPEDWRRF FLSPELTVQS VSGDNNVSGA
     TLKKQAAVIQ LINAWRTQGH LRAKLDPLGL NPPADVPSLQ PGFWGLSEED LLQEFSVTFG
     AHTTQMPLKQ LLNLLEQAWA GSQAYELAHL ENREEINWLL SRIESSNAPQ ADVQTCIARF
     EKLMAAETLE RYLHTRYVGQ KRFSLEGGES AIPALDTLTK RLRAQGVEEM VIGMAHRGRL
     NVLVNLLNKD PAQLFAEFEG KQTIGSGSGD VKYHMGYSSN LETPAGSLHV ALAYNPSHLE
     IVNPVVLGQV RARQERRGED GQAKVVGVLI HGDSALGGLG VNQTTFNLSQ TQGYGTGGTL
     HLVINNQIGF TTSRLQDMRS SRYCTDIAKM VAAPIIHVNG DDVDAVCQVM ELACEWRDTF
     RRDIIIDICC FRKHGHNESD EPRLTQPQMY QAVDAHPGTL ARYGESLARR GLLTQAQQDE
     MTARYRDWLD SCQKREPQPL KPAIHSFSAN WYGLTNPHWS APVSTALPRQ KLAAYGEIIS
     TLPPDVVAHP TIKRQLALRQ DMAAGTQPID WGMAEMLAYA SLVDAGVGVR LSGEDSGRGT
     FSHRHAVVHH QTEARRYLPL QHIRAGQASF DVYDSVLNEE ALLAFEYGYS TSAPQQLVIW
     EAQFGDFANG AQVAIDQFIS SGETKWDRYS GLTILLPHGY DGQGPEHSSA RPERWLQLCA
     ENNMQVVMPS ESAQMFHLLR GQALRPMRKP LVIMMSKRLL RFKGAMSELS EFTDGAYKPV
     ITDPQLHQPQ KVKRVILCSG QVYYDVLEAR KQRECEDEVA IVRLEQLYPF PVAELNDVLA
     SWPNCCEWIW LQEEPENQGA WRQIRHELAA LKINTPYWQY AGRPAAAAPA TGYGRVHKQQ
     IDEFLAAAFA DIQP
//