FOLM_ECOLI
ID FOLM_ECOLI Reviewed; 240 AA.
AC P0AFS3; P52109; P77386;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dihydromonapterin reductase {ECO:0000303|PubMed:19897652};
DE Short=H(2)-MPt reductase {ECO:0000303|PubMed:19897652};
DE EC=1.5.1.50 {ECO:0000269|PubMed:19897652};
DE AltName: Full=Dihydrofolate reductase {ECO:0000303|PubMed:14617668};
DE Short=DHFR;
DE EC=1.5.1.3 {ECO:0000269|PubMed:14617668};
GN Name=folM {ECO:0000303|PubMed:14617668}; Synonyms=ydgB;
GN OrderedLocusNames=b1606, JW1598;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-240.
RC STRAIN=K12;
RA Kuempel P.L.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14617668; DOI=10.1128/jb.185.23.7015-7018.2003;
RA Giladi M., Altman-Price N., Levin I., Levy L., Mevarech M.;
RT "FolM, a new chromosomally encoded dihydrofolate reductase in Escherichia
RT coli.";
RL J. Bacteriol. 185:7015-7018(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19897652; DOI=10.1128/jb.01198-09;
RA Pribat A., Blaby I.K., Lara-Nunez A., Gregory J.F., de Crecy-Lagard V.,
RA Hanson A.D.;
RT "FolX and FolM are essential for tetrahydromonapterin synthesis in
RT Escherichia coli and Pseudomonas aeruginosa.";
RL J. Bacteriol. 192:475-482(2010).
CC -!- FUNCTION: Catalyzes the reduction of dihydromonapterin to
CC tetrahydromonapterin. Also has lower activity with dihydrofolate.
CC {ECO:0000269|PubMed:19897652}.
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:0000269|PubMed:14617668};
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:0000269|PubMed:19897652};
CC -!- ACTIVITY REGULATION: Inhibited by methotrexate.
CC {ECO:0000269|PubMed:14617668}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 uM for 7,8-dihydrofolate (at pH 6.0)
CC {ECO:0000269|PubMed:14617668};
CC KM=147 uM for 7,8-dihydromonapterin (at pH 6.0)
CC {ECO:0000269|PubMed:19897652};
CC KM=1.9 uM for NADPH (at pH 6.0) {ECO:0000269|PubMed:14617668};
CC Vmax=0.083 umol/min/mg enzyme with 7,8-dihydrofolate as substrate
CC {ECO:0000269|PubMed:14617668};
CC Vmax=5.99 umol/min/mg enzyme with 7,8-dihydromoapterin as substrate
CC {ECO:0000269|PubMed:19897652};
CC pH dependence:
CC Optimum pH is 4.7. {ECO:0000269|PubMed:14617668};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FolM subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74678.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15344.1; -; Genomic_DNA.
DR EMBL; U41101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H64916; H64916.
DR RefSeq; NP_416123.1; NC_000913.3.
DR RefSeq; WP_000520804.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0AFS3; -.
DR SMR; P0AFS3; -.
DR BioGRID; 4262123; 119.
DR DIP; DIP-47981N; -.
DR IntAct; P0AFS3; 5.
DR STRING; 511145.b1606; -.
DR jPOST; P0AFS3; -.
DR PaxDb; P0AFS3; -.
DR PRIDE; P0AFS3; -.
DR EnsemblBacteria; AAC74678; AAC74678; b1606.
DR EnsemblBacteria; BAA15344; BAA15344; BAA15344.
DR GeneID; 949096; -.
DR KEGG; ecj:JW1598; -.
DR KEGG; eco:b1606; -.
DR PATRIC; fig|1411691.4.peg.656; -.
DR EchoBASE; EB2981; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR InParanoid; P0AFS3; -.
DR OMA; QIHVHAP; -.
DR PhylomeDB; P0AFS3; -.
DR BioCyc; EcoCyc:G6862-MON; -.
DR BioCyc; MetaCyc:G6862-MON; -.
DR BRENDA; 1.5.1.50; 2026.
DR SABIO-RK; P0AFS3; -.
DR PRO; PR:P0AFS3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IDA:EcoCyc.
DR GO; GO:0071172; F:dihydromonapterin reductase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR GO; GO:0042559; P:pteridine-containing compound biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW NADP; One-carbon metabolism; Oxidoreductase; Reference proteome.
FT CHAIN 1..240
FT /note="Dihydromonapterin reductase"
FT /id="PRO_0000054833"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT CONFLICT 210
FT /note="E -> Q (in Ref. 4)"
FT /evidence="ECO:0000305"
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
