FOLM_SHIDS
ID FOLM_SHIDS Reviewed; 240 AA.
AC Q32G72;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=SDY_1547;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB61683.1; -; Genomic_DNA.
DR RefSeq; WP_000520804.1; NC_007606.1.
DR RefSeq; YP_403174.1; NC_007606.1.
DR AlphaFoldDB; Q32G72; -.
DR SMR; Q32G72; -.
DR STRING; 300267.SDY_1547; -.
DR EnsemblBacteria; ABB61683; ABB61683; SDY_1547.
DR KEGG; sdy:SDY_1547; -.
DR PATRIC; fig|300267.13.peg.1856; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; QIHVHAP; -.
DR Proteomes; UP000002716; 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_0000339400"
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
