ID DYR_STAAM Reviewed; 159 AA. AC P0A016; P10167; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-JUN-2009, entry version 31. DE RecName: Full=Dihydrofolate reductase; DE Short=DHFR; DE EC=1.5.1.3; GN Name=folA; OrderedLocusNames=SAV1426; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). 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; BA000017; BAB57588.1; -; Genomic_DNA. DR RefSeq; NP_371950.1; -. DR HSSP; P00379; 1DHI. DR World-2DPAGE; 0002:P0A016; -. DR GeneID; 1121401; -. DR GenomeReviews; BA000017_GR; SAV1426. DR KEGG; sav:SAV1426; -. DR HOGENOM; P0A016; -. DR OMA; P0A016; HANAMYL. DR BioCyc; SAUR158878:SAV1426-MON; -. DR BindingDB; P0A016; -. 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 Complete proteome; NADP; One-carbon metabolism; Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 159 Dihydrofolate reductase. FT /FTId=PRO_0000186407. 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 //