ID DYR_ENCCU Reviewed; 205 AA. AC O62583; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 28-JUN-2023, entry version 117. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=DHFR-1; OrderedLocusNames=ECU01_0170; GN and GN Name=DHFR-2; OrderedLocusNames=ECU01_1450; GN and GN Name=DHFR-3; OrderedLocusNames=ECU08_0080; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11013707; DOI=10.1089/omi.1.1998.3.1; RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.; RT "First report on the systematic sequencing of the small genome of RT Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3 RT kbp region on chromosome I."; RL Microb. Comp. Genomics 3:1-11(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11157783; DOI=10.1101/gr.164301; RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., RA Weissenbach J., Saurin W., Vivares C.P.; RT "Sequence and analysis of chromosome I of the amitochondriate intracellular RT parasite Encephalitozoon cuniculi (Microspora)."; RL Genome Res. 11:198-207(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). 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; AJ005644; CAA06647.1; -; Genomic_DNA. DR EMBL; AL391737; CAD24887.1; -; Genomic_DNA. DR EMBL; AL391737; CAD25017.1; -; Genomic_DNA. DR EMBL; AL590448; CAD26313.1; -; Genomic_DNA. DR RefSeq; NP_597137.1; NM_001041746.1. DR RefSeq; XP_965852.1; XM_960759.1. DR RefSeq; XP_965982.1; XM_960889.1. DR AlphaFoldDB; O62583; -. DR SMR; O62583; -. DR STRING; 284813.O62583; -. DR GeneID; 859559; -. DR KEGG; ecu:ECU08_0080; -. DR VEuPathDB; MicrosporidiaDB:ECU01_0170; -. DR VEuPathDB; MicrosporidiaDB:ECU01_1450; -. DR VEuPathDB; MicrosporidiaDB:ECU08_0080; -. DR HOGENOM; CLU_043966_2_1_1; -. DR InParanoid; O62583; -. DR OMA; NANALPW; -. DR OrthoDB; 1118873at2759; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000819; Chromosome I. DR Proteomes; UP000000819; Chromosome VIII. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. 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; IEA:UniProtKB-UniPathway. 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; 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; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW NADP; One-carbon metabolism; Oxidoreductase; Reference proteome. FT CHAIN 1..205 FT /note="Dihydrofolate reductase" FT /id="PRO_0000186373" FT DOMAIN 1..201 FT /note="DHFR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660" FT BINDING 7 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 13..19 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 62..64 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 84..86 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 118..125 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" SQ SEQUENCE 205 AA; 22883 MW; 45450EAA534487DD CRC64; MLALVVALAS HRGIGNANAL PWPRPLAADM AWFRTLSQSI PLISPDRIAL APSASNAVVM GRRTWDSIPS RFRPLANRIN VVLSRGPARS TENTFFIQTF EALDSLPLPP SSMTFVIGGR DVYSLALESG RPHLIFATEV FESPECDVFF PHIDWASYEK RDITRDVSRL IDRTLASAFY SPETATFTEN GTSFKMFLYT KPETR //