ID   DYR_STAEQ               Reviewed;         161 AA.
AC   Q5HPB1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-NOV-2008, entry version 30.
DE   RecName: Full=Dihydrofolate reductase;
DE            Short=DHFR;
DE            EC=1.5.1.3;
GN   Name=folA; Synonyms=dfrC, folA1; OrderedLocusNames=SERP1002;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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.
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DR   EMBL; CP000029; AAW54371.1; -; Genomic_DNA.
DR   RefSeq; YP_188579.1; -.
DR   GeneID; 3242034; -.
DR   GenomeReviews; CP000029_GR; SERP1002.
DR   KEGG; ser:SERP1002; -.
DR   TIGR; SERP1002; -.
DR   HOGENOM; Q5HPB1; -.
DR   BioCyc; SEPI176279:SERP1002-MON; -.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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   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    161       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186415.
FT   DOMAIN        2    157       DHFR.
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
//