ID DYR_CAEEL Reviewed; 189 AA. AC Q93341; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Putative dihydrofolate reductase; DE EC=1.5.1.3; GN Name=dhfr-1; ORFNames=C36B1.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z80215; CAB02272.1; -; Genomic_DNA. DR PIR; T19778; T19778. DR RefSeq; NP_492364.1; NM_059963.3. DR AlphaFoldDB; Q93341; -. DR SMR; Q93341; -. DR BioGRID; 38114; 2. DR IntAct; Q93341; 1. DR STRING; 6239.C36B1.7.1; -. DR EPD; Q93341; -. DR PaxDb; 6239-C36B1-7; -. DR PeptideAtlas; Q93341; -. DR EnsemblMetazoa; C36B1.7.1; C36B1.7.1; WBGene00007974. DR GeneID; 172681; -. DR KEGG; cel:CELE_C36B1.7; -. DR UCSC; C36B1.7; c. elegans. DR AGR; WB:WBGene00007974; -. DR WormBase; C36B1.7; CE05374; WBGene00007974; dhfr-1. DR eggNOG; KOG1324; Eukaryota. DR GeneTree; ENSGT00940000168797; -. DR HOGENOM; CLU_043966_2_3_1; -. DR InParanoid; Q93341; -. DR OMA; QYEFQMW; -. DR OrthoDB; 1118873at2759; -. DR PhylomeDB; Q93341; -. DR Reactome; R-CEL-196757; Metabolism of folate and pterines. DR UniPathway; UPA00077; UER00158. DR PRO; PR:Q93341; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00007974; Expressed in germ line (C elegans) and 4 other cell types or tissues. 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; Dihydrofolate Reductase, subunit A; 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; DIHYDROFOLATE REDUCTASE; 1. DR PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW NADP; One-carbon metabolism; Oxidoreductase; Reference proteome. FT CHAIN 1..189 FT /note="Putative dihydrofolate reductase" FT /id="PRO_0000186372" FT DOMAIN 3..185 FT /note="DHFR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660" FT BINDING 9 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 15..21 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 29..34 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 53..55 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 75..77 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 115..122 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" SQ SEQUENCE 189 AA; 21602 MW; C1642558E097725F CRC64; MRKMNLIVAM DAEGGIGKNG VLPWRIKKDM QYFASVTKNV SDQSKRNAVL MGRKCWESIP VTRRPLAGRL NIVLSRQLPA QKSDDYIVVN SLEAAMKLLS EPPFVDSIET IWNIGGAEIY DLALRENLVD EIHLTRIFKN FEADVHLKSL DFSKMEKVQN AEVSSENSEI FEENGLKFEF CKWKVVENH //