ID   FOLM_ECOHS              Reviewed;         240 AA.
AC   A8A0E8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=EcHS_A1681;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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}.
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DR   EMBL; CP000802; ABV06002.1; -; Genomic_DNA.
DR   RefSeq; WP_000520804.1; NC_009800.1.
DR   AlphaFoldDB; A8A0E8; -.
DR   SMR; A8A0E8; -.
DR   KEGG; ecx:EcHS_A1681; -.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OMA; QIHVHAP; -.
DR   Proteomes; UP000001123; 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_0000339397"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   240 AA;  26348 MW;  73B942EE144E2CC3 CRC64;
     MGKTQPLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLINA GAQCIQADFS
     TNDGVMAFAD EVLKSTHGLR AILHNASAWM AEKPGAPLAD VLACMMQIHV NTPYLLNHAL
     ERLLRGHGHA ASDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNSIA
     PSLILFNEHD DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR