ID   DYR_CRYNE               Reviewed;         229 AA.
AC   Q07801; Q5KAF0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Dihydrofolate reductase;
DE            EC=1.5.1.3;
GN   Name=DFR1; Synonyms=DHFR; OrderedLocusNames=CNJ01940;
OS   Cryptococcus neoformans (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella;
OC   Filobasidiella/Cryptococcus neoformans species complex.
OX   NCBI_TaxID=5207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND
RP   CHARACTERIZATION.
RX   MEDLINE=93232049; PubMed=8473332;
RA   Sirawaraporn W., Cao M., Santi D.V., Edman J.C.;
RT   "Cloning, expression, and characterization of Cryptococcus neoformans
RT   dihydrofolate reductase.";
RL   J. Biol. Chem. 268:8888-8892(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J.,
RA   D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J.,
RA   Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I.,
RA   Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E.,
RA   Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L.,
RA   Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A.,
RA   Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R.,
RA   Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W.,
RA   Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen
RT   Cryptococcus neoformans.";
RL   Science 307:1321-1324(2005).
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   -!- SUBUNIT: Monomer.
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; S58802; AAB26198.1; -; Genomic_DNA.
DR   EMBL; AE017350; AAW45849.1; ALT_INIT; Genomic_DNA.
DR   PIR; A46049; A46049.
DR   RefSeq; XP_567366.1; -.
DR   HSSP; P13922; 1J3K.
DR   GeneID; 3254250; -.
DR   GenomeReviews; AE017350_GR; CNJ01940.
DR   KEGG; cne:CNJ01940; -.
DR   HOGENOM; Q07801; -.
DR   BRENDA; 1.5.1.3; 2772.
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; Direct protein sequencing; NADP;
KW   One-carbon metabolism; Oxidoreductase.
FT   CHAIN         1    229       Dihydrofolate reductase.
FT                                /FTId=PRO_0000186375.
FT   DOMAIN       11    227       DHFR.
SQ   SEQUENCE   229 AA;  25169 MW;  60D9E4FF66C5F198 CRC64;
     MQTTAKSSTP SITAVVAATA ENGIGLNGGL PWRLPGEMKY FARVTTGETP SSDPSEQNVV
     IMGRKTWESI PSRFRPLKNR RNVVISGKGV DLGTAENSTV YTDIPSALSA LRSTTESGHS
     PRIFLIGGAT LYTSSLLPSS VPSLNSSTST SPLPFSRPLI DRILLTRILS PFECDAYLED
     FAAHTKPDGS KVWKKASIKE FREWIGWDIE EQVEEKGVKY IFEMWVLNQ
//