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Database: UniProt/TrEMBL
Entry: C8TTX5_ECO26
LinkDB: C8TTX5_ECO26
Original site: C8TTX5_ECO26 
ID   C8TTX5_ECO26            Unreviewed;       361 AA.
AC   C8TTX5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   26-NOV-2014, entry version 36.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|RuleBase:RU004473};
DE            EC=4.2.1.46 {ECO:0000256|RuleBase:RU004473};
GN   Name=rmlB {ECO:0000313|EMBL:BAI26175.1};
GN   OrderedLocusNames=ECO26_2952 {ECO:0000313|EMBL:BAI26175.1};
OS   Escherichia coli O26:H11 (strain 11368 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=573235 {ECO:0000313|EMBL:BAI26175.1, ECO:0000313|Proteomes:UP000001617};
RN   [1] {ECO:0000313|EMBL:BAI26175.1, ECO:0000313|Proteomes:UP000001617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11368 / EHEC {ECO:0000313|Proteomes:UP000001617};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-
CC       alpha-D-glucose + H(2)O. {ECO:0000256|RuleBase:RU004473}.
CC   -!- COFACTOR:
CC       Note=NAD. {ECO:0000256|RuleBase:RU004473};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily.
CC       {ECO:0000256|RuleBase:RU004473}.
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DR   EMBL; AP010953; BAI26175.1; -; Genomic_DNA.
DR   RefSeq; YP_003229915.1; NC_013361.1.
DR   ProteinModelPortal; C8TTX5; -.
DR   SMR; C8TTX5; 1-352.
DR   STRING; 573235.ECO26_2952; -.
DR   EnsemblBacteria; BAI26175; BAI26175; ECO26_2952.
DR   GeneID; 8482389; -.
DR   KEGG; eoj:ECO26_2952; -.
DR   PATRIC; 18401556; VBIEscCol24965_3014.
DR   eggNOG; COG1088; -.
DR   HOGENOM; HOG000168006; -.
DR   KO; K01710; -.
DR   OrthoDB; EOG6PZXCX; -.
DR   BioCyc; ECOL573235:GCY7-3035-MONOMER; -.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR   InterPro; IPR001509; Epimerase_deHydtase_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR10366:SF41; PTHR10366:SF41; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001617};
KW   Lyase {ECO:0000256|RuleBase:RU004473}.
SQ   SEQUENCE   361 AA;  40533 MW;  D5DBE79A268F0550 CRC64;
     MKILVTGGAG FIGSAVVRHI INNTQDSVVN VDKLTYAGNL ESLADVSDSE RYVFEHADIC
     DAAAMARIFA QHQPDAVMHL AAESHVDRSI TGPAAFIETN IVGTYVLLEA ARNYWSALDS
     DKKNSFRFHH ISTDEVYGDL PHPDEVNNTE ELPLFTETTA YAPSSPYSAS KASSDHLVRA
     WKRTYGLPTI VTNCSNNYGP YHFPEKLIPL VILNALEGKA LPIYGKGDQI RDWLYVEDHA
     RALYTVVTEG KAGETYNIGG HNEKKNIDVV LTICDLLDEI VPKEQSYREQ ITYVADRPGH
     DRRYAIDAEK ISRELGWKPQ ETFESGIRKT VEWYLSNTKW VENVKSGAYQ SWIAQNYEGR
     Q
//
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