ID B7UPL5_ECO27 Unreviewed; 914 AA.
AC B7UPL5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC 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};
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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: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: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
//
