ID   DYR_STAAU               Reviewed;         159 AA.
AC   P0A017; P10167;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Dihydrofolate reductase;
DE            Short=DHFR;
DE            EC=1.5.1.3;
GN   Name=folA;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413;
RX   MEDLINE=93371025; PubMed=8363365;
RA   Dale G.E., Then R.L., Stueber D.;
RT   "Characterization of the gene for chromosomal trimethoprim-sensitive
RT   dihydrofolate reductase of Staphylococcus aureus ATCC 25923.";
RL   Antimicrob. Agents Chemother. 37:1400-1405(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36.
RC   STRAIN=157/4696;
RX   MEDLINE=89078604; PubMed=3060373; DOI=10.1016/0014-5793(88)81006-8;
RA   Hartman P.G., Stahli M., Kocher H.P., Then R.L.;
RT   "N-terminal amino acid sequence of the chromosomal dihydrofolate
RT   reductase purified from trimethoprim-resistant Staphylococcus
RT   aureus.";
RL   FEBS Lett. 242:157-160(1988).
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: There are two dhfR isozymes in S.aureus, this one
CC       is chromosomal and is sensitive to trimethoprim.
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; Z16422; CAA78910.1; -; Genomic_DNA.
DR   PIR; S32014; S32014.
DR   PDB; 2W9G; X-ray; 1.95 A; A=1-159.
DR   PDB; 2W9H; X-ray; 1.48 A; A=1-159.
DR   PDBsum; 2W9G; -.
DR   PDBsum; 2W9H; -.
DR   BRENDA; 1.5.1.3; 95.
DR   BindingDB; P0A017; -.
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   3D-structure; Direct protein sequencing; NADP; One-carbon metabolism;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    159       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186411.
FT   DOMAIN        2    157       DHFR.
SQ   SEQUENCE   159 AA;  18251 MW;  811898409FEAFAAB CRC64;
     MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES IGKPLPNRRN
     VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE EMIDKVDDMY ITVIEGKFRG
     DTFFPPYTFE DWEVASSVEG KLDEKNTIPH TFLHLIRKK
//