ID DYR_BOVIN Reviewed; 187 AA. AC P00376; Q29RI1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 55. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=DHFR; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Heart ventricle; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-187. RC TISSUE=Liver; RX MEDLINE=83000246; PubMed=7115669; DOI=10.1021/bi00257a006; RA Lai P.-H., Pan Y.-C.E., Gleisner J.M., Peterson D.L., Williams K.R., RA Blakley R.L.; RT "Structure of dihydrofolate reductase: primary sequence of the bovine RT liver enzyme."; RL Biochemistry 21:3284-3294(1982). 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; BC114162; AAI14163.1; -; mRNA. DR PIR; A00388; RDBOD. DR RefSeq; NP_001071351.1; -. DR UniGene; Bt.18730; -. DR HSSP; P00374; 1DHF. DR SMR; P00376; 2-187. DR Ensembl; ENSBTAG00000007681; Bos taurus. DR GeneID; 508809; -. DR KEGG; bta:508809; -. DR HOVERGEN; P00376; -. DR GO; GO:0004146; F:dihydrofolate reductase activity; 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; IPR001796; DHFR_reg. 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 Direct protein sequencing; NADP; One-carbon metabolism; KW Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 187 Dihydrofolate reductase. FT /FTId=PRO_0000186361. FT DOMAIN 4 185 DHFR. FT CONFLICT 22 22 D -> N (in Ref. 1; AAI14163). FT CONFLICT 102 102 E -> Q (in Ref. 2; AA sequence). SQ SEQUENCE 187 AA; 21604 MW; 0727DD855C8A7CD8 CRC64; MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFQYFQRMTT VSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPKGAHFL AKSLDDALEL IEDPELTNKV DVVWIVGGSS VYKEAMNKPG HVRLFVTRIM QEFESDAFFP EIDFEKYKLL PEYPGVPLDV QEEKGIKYKF EVYEKNN //