ID   FOLM_ECOL6              Reviewed;         240 AA.
AC   Q8FHB1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=c1998;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80458.1; -; Genomic_DNA.
DR   RefSeq; WP_000520812.1; NC_004431.1.
DR   AlphaFoldDB; Q8FHB1; -.
DR   SMR; Q8FHB1; -.
DR   STRING; 199310.c1998; -.
DR   EnsemblBacteria; AAN80458; AAN80458; c1998.
DR   KEGG; ecc:c1998; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OMA; QIHVHAP; -.
DR   BioCyc; ECOL199310:C1998-MON; -.
DR   Proteomes; UP000001410; 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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 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_0000339395"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   240 AA;  26348 MW;  72A9A8E1D7EB6C4C CRC64;
     MGKTQSLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLIKA GAQCIQADFS
     TNDGVMAFAD EVLKSTHGLR AILHNASAWM AEKPGAPLTD VLACMMQIHV NTPYLLNHAL
     ERLLRGHGHA ASDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNSIA
     PSLILFNEHD DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS LPLDGGRHLR