ID Q2IYG6_RHOP2 Unreviewed; 179 AA. AC Q2IYG6; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194}; DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194}; GN OrderedLocusNames=RPB_2037 {ECO:0000313|EMBL:ABD06744.1}; OS Rhodopseudomonas palustris (strain HaA2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD06744.1, ECO:0000313|Proteomes:UP000008809}; RN [1] {ECO:0000313|EMBL:ABD06744.1, ECO:0000313|Proteomes:UP000008809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD06744.1, RC ECO:0000313|Proteomes:UP000008809}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A., RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris HaA2."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|ARBA:ARBA00025067, CC ECO:0000256|PIRNR:PIRNR000194}. 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; CC Evidence={ECO:0000256|PIRNR:PIRNR000194}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8- CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC {ECO:0000256|ARBA:ARBA00004903, ECO:0000256|PIRNR:PIRNR000194}. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC {ECO:0000256|ARBA:ARBA00009539, ECO:0000256|PIRNR:PIRNR000194, CC ECO:0000256|RuleBase:RU004474}. 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; CP000250; ABD06744.1; -; Genomic_DNA. DR AlphaFoldDB; Q2IYG6; -. DR STRING; 316058.RPB_2037; -. DR KEGG; rpb:RPB_2037; -. DR eggNOG; COG0262; Bacteria. DR HOGENOM; CLU_043966_5_1_5; -. DR OrthoDB; 9804315at2; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000008809; Chromosome. 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; 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 PIRSF; PIRSF000194; DHFR; 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 {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000194}; KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000194}. FT DOMAIN 11..175 FT /note="DHFR" FT /evidence="ECO:0000259|PROSITE:PS51330" SQ SEQUENCE 179 AA; 19532 MW; DE7E53E1325F87FC CRC64; MSSPGVSSRL SIVLIVAVAD NGVIGRDNAI PWRLKSDLQR FKQLTLNKPI IMGRKTYQSI GRPLPGRTNI VVTRDPTFHA DGVVVVPSFD AAEQVACGDA MRRFATEIAV IGGAEIYAHW LPRATRIELT EVHASPPGDA TFPALDPSQW EETARTHHAA GPQDSADVSY VTYRRCTAR //