ID   DYR_SHV21               Reviewed;         187 AA.
AC   P09503;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Viral dihydrofolate reductase;
DE            Short=vDHFR;
DE            EC=1.5.1.3;
GN   Name=DHFR; Synonyms=2;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC   Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88145671; PubMed=2830673; DOI=10.1126/science.2830673;
RA   Trimble J.J., Murthy S.C.S., Bakker A., Grassmann R., Desrosiers R.C.;
RT   "A gene for dihydrofolate reductase in a herpesvirus.";
RL   Science 239:1145-1147(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89311619; PubMed=2545905;
RA   Murthy S.C.S., Trimble J.J., Desrosiers R.C.;
RT   "Deletion mutants of herpesvirus saimiri define an open reading frame
RT   necessary for transformation.";
RL   J. Virol. 63:3307-3314(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=92333688; PubMed=1321287;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
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; X64346; CAA45624.1; -; Genomic_DNA.
DR   EMBL; M28071; AAA58726.1; -; Genomic_DNA.
DR   EMBL; M19237; AAA46154.1; -; Genomic_DNA.
DR   RefSeq; NP_040203.1; -.
DR   HSSP; P00374; 1DHF.
DR   SMR; P09503; 2-186.
DR   GeneID; 1488256; -.
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   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    187       Viral dihydrofolate reductase.
FT                                /FTId=PRO_0000186380.
FT   DOMAIN        4    185       DHFR.
SQ   SEQUENCE   187 AA;  21719 MW;  46666EAA3BEA5140 CRC64;
     MVQALNCIVA VAQNMGIGKQ GNLPWPRLMN DFKHFQRMTT TSSVPDKQNL VIMGKKTWFS
     IPEKNRPLKG RINVVLSKEL KELPHRAHFL AKSLDDALKL TEQPELANKV DMVWIIGGSS
     VYKEAMSYPC DLKLFVTRIM QDFECDTFFP EFDLEKYKLL IEYPSVLSNV QEEKSIKYKF
     EVYEKNH
//