DYR_SCHPO
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 03-AUG-2022, entry version 147.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=dfr1; ORFNames=SPCC1223.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; L13703; AAA57051.1; -; mRNA.
DR EMBL; CU329672; CAA20877.1; -; Genomic_DNA.
DR PIR; T43248; T43248.
DR RefSeq; NP_588353.1; NM_001023344.2.
DR AlphaFoldDB; P36591; -.
DR SMR; P36591; -.
DR BioGRID; 275621; 8.
DR STRING; 4896.SPCC1223.08c.1; -.
DR ESTHER; schpo-dyr; FSH1.
DR iPTMnet; P36591; -.
DR MaxQB; P36591; -.
DR PaxDb; P36591; -.
DR PRIDE; P36591; -.
DR EnsemblFungi; SPCC1223.08c.1; SPCC1223.08c.1:pep; SPCC1223.08c.
DR GeneID; 2539048; -.
DR KEGG; spo:SPCC1223.08c; -.
DR PomBase; SPCC1223.08c; dfr1.
DR VEuPathDB; FungiDB:SPCC1223.08c; -.
DR eggNOG; KOG1324; Eukaryota.
DR eggNOG; KOG2551; Eukaryota.
DR HOGENOM; CLU_627245_0_0_1; -.
DR InParanoid; P36591; -.
DR OMA; HIVPQQA; -.
DR Reactome; R-SPO-196757; Metabolism of folate and pterines.
DR UniPathway; UPA00077; UER00158.
DR PRO; PR:P36591; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IGI:PomBase.
DR GO; GO:0004622; F:lysophospholipase activity; TAS:PomBase.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0046452; P:dihydrofolate metabolic process; ISO:PomBase.
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:0006629; P:lipid metabolic process; TAS:PomBase.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISO:PomBase.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR005645; FSH_dom.
DR PANTHER; PTHR48069; PTHR48069; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR Pfam; PF03959; FSH1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; NADP; Nucleotide-binding; One-carbon metabolism;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..461
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186377"
FT DOMAIN 233..447
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 246..252
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 260..265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292..294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 365..372
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 126..127
FT /note="QP -> HA (in Ref. 1; AAA57051)"
FT /evidence="ECO:0000305"
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
