ID FOLM_ENT38 Reviewed; 240 AA. AC A4W9Z4; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Dihydromonapterin reductase; DE Short=H(2)-MPt reductase; DE EC=1.5.1.50 {ECO:0000250|UniProtKB:P0AFS3}; DE AltName: Full=Dihydrofolate reductase; DE Short=DHFR; DE EC=1.5.1.3 {ECO:0000250|UniProtKB:P0AFS3}; GN Name=folM; OrderedLocusNames=Ent638_1846; OS Enterobacter sp. (strain 638). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638; RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943; RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., RA Vangronsveld J., Newman L., Monchy S.; RT "Genome sequence of the plant growth promoting endophytic bacterium RT Enterobacter sp. 638."; RL PLoS Genet. 6:E1000943-E1000943(2010). CC -!- FUNCTION: Catalyzes the reduction of dihydromonapterin to CC tetrahydromonapterin. Also has lower activity with dihydrofolate. CC {ECO:0000250|UniProtKB:P0AFS3}. 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:0000250|UniProtKB:P0AFS3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7,8-dihydromonapterin + H(+) + NADPH = 5,6,7,8- CC tetrahydromonapterin + NADP(+); Xref=Rhea:RHEA:34847, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:71175, ChEBI:CHEBI:71177; EC=1.5.1.50; CC Evidence={ECO:0000250|UniProtKB:P0AFS3}; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. FolM subfamily. {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; CP000653; ABP60524.1; -; Genomic_DNA. DR RefSeq; WP_012017239.1; NC_009436.1. DR AlphaFoldDB; A4W9Z4; -. DR SMR; A4W9Z4; -. DR STRING; 399742.Ent638_1846; -. DR KEGG; ent:Ent638_1846; -. DR eggNOG; COG1028; Bacteria. DR HOGENOM; CLU_010194_1_3_6; -. DR OrthoDB; 9793499at2; -. DR Proteomes; UP000000230; Chromosome. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43639:SF6; DIHYDROMONAPTERIN REDUCTASE; 1. DR PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW NADP; One-carbon metabolism; Oxidoreductase. FT CHAIN 1..240 FT /note="Dihydromonapterin reductase" FT /id="PRO_0000339389" FT ACT_SITE 152 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" SQ SEQUENCE 240 AA; 26370 MW; 4548F2A04F03AF87 CRC64; MGNAPQRPIL ITGGGRRIGL ALAHHFLTLR QPVIVSYRNE YPSIEGLRQA GATCIQADFS TDEGILRFAE TVKSNTRGLR AIIHNASAWQ AEKPGTPLSE TLACMMQIHV HAPYLLNHAL EELLRGHGHA AGDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNAIA PSLILFNEED DAEYRQKALN KSLMKIVPGE KEVIDLIDYL LTSCYVTGRS FGVDGGRPLN //