ID DYR_ECOL6 Reviewed; 159 AA. AC P0ABQ5; P00379; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; OrderedLocusNames=c0058; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC tetrahydrofolate from dihydrofolate: step 1/1. CC -!- MISCELLANEOUS: The reaction catalyzed by this enzyme represents an CC essential step for de novo glycine and purine synthesis, DNA CC precursor synthesis, and for the conversion of dUMP to dTMP. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014075; AAN78554.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_752010.1; -. DR SMR; P0ABQ5; 1-159. DR DisProt; DP00301; -. DR GeneID; 1035973; -. DR GenomeReviews; AE014075_GR; c0058. DR KEGG; ecc:c0058; -. DR HOGENOM; P0ABQ5; -. DR OMA; P0ABQ5; WKEAERT. DR BRENDA; 1.5.1.3; 292881. DR BindingDB; P0ABQ5; -. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:EC. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR012259; DHFR. DR InterPro; IPR001796; DHFR_reg. DR InterPro; IPR017925; Dihydrofolate_reductase_CS. DR PANTHER; PTHR11549:SF1; DHFR; 1. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; One-carbon metabolism; Oxidoreductase. FT CHAIN 1 159 Dihydrofolate reductase. FT /FTId=PRO_0000186388. FT DOMAIN 1 158 DHFR. SQ SEQUENCE 159 AA; 17999 MW; 6A03CDCD7F5F8562 CRC64; MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR //