ID   DYR_SCHPO               Reviewed;         461 AA.
AC   P36591; O74408;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-NOV-2008, entry version 58.
DE   RecName: Full=Dihydrofolate reductase;
DE            EC=1.5.1.3;
GN   Name=dfr1; ORFNames=SPCC1223.08c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94374697; PubMed=8088538; DOI=10.1016/0378-1119(94)90052-3;
RA   Bertani L.E., Campbell J.L.;
RT   "The isolation and characterization of the gene (dfr1) encoding
RT   dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe.";
RL   Gene 147:131-135(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; L13703; AAA57051.1; -; mRNA.
DR   EMBL; CU329672; CAA20877.1; -; Genomic_DNA.
DR   PIR; T43248; T43248.
DR   RefSeq; NP_588353.1; -.
DR   HSSP; P16184; 1DYR.
DR   GeneID; 2539048; -.
DR   KEGG; spo:SPCC1223.08c; -.
DR   NMPDR; fig|4896.1.peg.691; -.
DR   GeneDB_Spombe; SPCC1223.08c; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000273-MON; -.
DR   ArrayExpress; P36591; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   InterPro; IPR005645; DUF341.
DR   Pfam; PF00186; DHFR_1; 1.
DR   Pfam; PF03959; FSH1; 1.
DR   PRINTS; PR00070; DHFR.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; NADP; Nucleotide-binding;
KW   One-carbon metabolism; Oxidoreductase.
FT   CHAIN         1    461       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186377.
FT   DOMAIN      233    447       DHFR.
FT   NP_BIND     275    282       ATP (Potential).
FT   CONFLICT    126    127       QP -> HA (in Ref. 1; AAA57051).
SQ   SEQUENCE   461 AA;  51523 MW;  F6A3695F537A03C9 CRC64;
     MSKPLKVLCL HGWIQSGPVF SKKMGSVQKY LSKYAELHFP TGPVVADEEA DPNDEEEKKR
     LAALGGEQNG GKFGWFEVED FKNTYGSWDE SLECINQYMQ EKGPFDGLIG FSQGAGIGAM
     LAQMLQPGQP PNPYVQHPPF KFVVFVGGFR AEKPEFDHFY NPKLTTPSLH IAGTSDTLVP
     LARSKQLVER CENAHVLLHP GQHIVPQQAV YKTGIRDFMF SAPTKEPTKH PRDLTMIVAV
     SSPNLGIGKK NSMPWHIKQE MAYFANVTSS TESSGQLEEG KSKIMNVVIM GRSCYDSLPK
     KNRPLKDRIN IVITRNSNYN FGLTKKEKMP ENLYAADCID SALDLVAEKY GADSDIQVGK
     VFIIGGSFLY GSALYHPLTK NLLFTRIHKE YPCDSFFPFE PAESSDWVRK AHPELEKFVG
     IPVEEGRLKA ASSNKEEVEI EFELYGKNDD VNVALEKLSI C
//