FOLM_SHIFL
ID FOLM_SHIFL Reviewed; 240 AA.
AC Q83RC9; Q7C1H7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=SF1627, S1759;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43210.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17098.1; -; Genomic_DNA.
DR RefSeq; NP_707503.1; NC_004337.2.
DR RefSeq; WP_000520806.1; NZ_WPGW01000024.1.
DR AlphaFoldDB; Q83RC9; -.
DR SMR; Q83RC9; -.
DR STRING; 198214.SF1627; -.
DR EnsemblBacteria; AAN43210; AAN43210; SF1627.
DR EnsemblBacteria; AAP17098; AAP17098; S1759.
DR GeneID; 1024813; -.
DR GeneID; 58389277; -.
DR KEGG; sfl:SF1627; -.
DR KEGG; sfx:S1759; -.
DR PATRIC; fig|198214.7.peg.1921; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; QIHVHAP; -.
DR OrthoDB; 1821409at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT CHAIN 1..240
FT /note="Dihydromonapterin reductase"
FT /id="PRO_0000339401"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ SEQUENCE 240 AA; 26330 MW; 1A227307B826086A CRC64;
MGKTQPLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLINA GAQCIQADFS
TNDGVMAFAD EVLKTTHGLR AILHNASAWI AEKPGAPLAD VLACMMQIHV NTPYLLNHAL
ERLLRGHGHA ASDIIHFTDY VVERGSDKHV AYAASKAALD NMTRSFARKL APEVKVNSIA
PSLILFNEHD DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR
