DYR_CRYNJ
ID DYR_CRYNJ Reviewed; 229 AA.
AC Q07801; Q5KAF0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=DFR1; Synonyms=DHFR; OrderedLocusNames=CNJ01940;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND
RP CHARACTERIZATION.
RX PubMed=8473332; DOI=10.1016/s0021-9258(18)52956-2;
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 / ATCC MYA-565;
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., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC reaction for de novo glycine and purine synthesis, and for DNA
CC precursor synthesis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00660};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW45849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; XM_567366.1.
DR AlphaFoldDB; Q07801; -.
DR SMR; Q07801; -.
DR STRING; 5207.AAW45849; -.
DR PaxDb; Q07801; -.
DR EnsemblFungi; AAW45849; AAW45849; CNJ01940.
DR GeneID; 3254250; -.
DR KEGG; cne:CNJ01940; -.
DR eggNOG; KOG1324; Eukaryota.
DR InParanoid; Q07801; -.
DR OrthoDB; 1489621at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000002149; Chromosome 10.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0046452; P:dihydrofolate metabolic process; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR PANTHER; PTHR48069; PTHR48069; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
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; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186375"
FT DOMAIN 11..227
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 23..29
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 37..42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 127..134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
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
