ID DYR_UREPA Reviewed; 156 AA. AC Q9PR30; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; OrderedLocusNames=UU114; OS Ureaplasma parvum serovar 3 (strain ATCC 700970). OC Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Ureaplasma. OX NCBI_TaxID=273119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700970; RX PubMed=11048724; DOI=10.1038/35037619; RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., RA Cassell G.H.; RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum."; RL Nature 407:757-762(2000). 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 NADPH + H(+); 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; AF222894; AAF30520.1; -; Genomic_DNA. DR RefSeq; WP_006689146.1; NC_002162.1. DR AlphaFoldDB; Q9PR30; -. DR SMR; Q9PR30; -. DR STRING; 273119.UU114; -. DR EnsemblBacteria; AAF30520; AAF30520; UU114. DR GeneID; 29672261; -. DR KEGG; uur:UU114; -. DR eggNOG; COG0262; Bacteria. DR HOGENOM; CLU_043966_5_2_14; -. DR OrthoDB; 9804315at2; -. DR UniPathway; UPA00077; UER00158. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0046452; P:dihydrofolate metabolic process; IEA:TreeGrafter. DR GO; GO:0046655; P:folic acid metabolic process; IEA:TreeGrafter. 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. FT CHAIN 1..156 FT /note="Dihydrofolate reductase" FT /id="PRO_0000186419" FT DOMAIN 1..156 FT /note="DHFR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660" SQ SEQUENCE 156 AA; 18534 MW; 93A79ED2E62282AC CRC64; MLKLIWCQTL NGGISKNNKL PWYIKEELDH FYKTTKNHKI IMGKNTFDSL DQKPLNNRTN IIFSSIMQTP EDESYFVTND FQQVLNDAKK EDIFIIGGKE LFDIFLAYAD VLIVSVLKDY YDCDLYMKVD YNNFNLDKQD VYDNFIVNYY SNKKEK //