ID DYR_STAEP Reviewed; 161 AA. AC P0C0P0; Q59908; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Dihydrofolate reductase; DE Short=DHFR; DE EC=1.5.1.3; GN Name=folA; Synonyms=dfrC, folA1; OS Staphylococcus epidermidis. OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=1282; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS. RC STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55; RX MEDLINE=95286471; PubMed=7768789; RA Dale G.E., Broger C., Hartman P.G., Langen H., Page M.G.P., Then R.L., RA Stueber D.; RT "Characterization of the gene for the chromosomal dihydrofolate RT reductase (DHFR) of Staphylococcus epidermidis ATCC 14990: the origin RT of the trimethoprim-resistant S1 DHFR from Staphylococcus aureus?"; RL J. Bacteriol. 177:2965-2970(1995). CC -!- FUNCTION: Not resistant to trimethoprim. 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; Z48233; CAA88269.1; -; Genomic_DNA. DR PIR; A57271; A57271. DR HSSP; P00379; 1DHI. DR BRENDA; 1.5.1.3; 874. 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 1: Evidence at protein level; KW NADP; One-carbon metabolism; Oxidoreductase. FT CHAIN 1 161 Dihydrofolate reductase. FT /FTId=PRO_0000186413. FT DOMAIN 2 157 DHFR. FT MUTAGEN 32 32 V->I: 3-fold increase of KM for FT dihydrofolate. FT MUTAGEN 44 44 G->A: 5-fold increase of KM for NADPH. FT MUTAGEN 99 99 F->Y: Trimethoprim resistance. SQ SEQUENCE 161 AA; 18417 MW; CB3167940A387EE0 CRC64; MTLSIIVAHD KQRVIGYQNQ LPWHLPNDLK HVKQLTTGNT LVMGRKTFNS IGKPLPNRRN VVLTNQASFH HEGVDVINSL DEIKELSGHV FIFGGQTLFE AMIDQVDDMY ITVIDGKFQG DTFFPPYTFE NWEVESSVEG QLDEKNTIPH TFLHLVRRKG K //