FOLM_SHISS
ID FOLM_SHISS Reviewed; 240 AA.
AC Q3Z1V9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=SSON_1554;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
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}.
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DR EMBL; CP000038; AAZ88253.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z1V9; -.
DR SMR; Q3Z1V9; -.
DR EnsemblBacteria; AAZ88253; AAZ88253; SSON_1554.
DR KEGG; ssn:SSON_1554; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; QIHVHAP; -.
DR Proteomes; UP000002529; 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_0000339403"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ SEQUENCE 240 AA; 26328 MW; 749E62F921924298 CRC64;
MGKAQPLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLIKA GAQCIQADFS
TNDGVMAFAD EVLKSPHGLR AILHNASAWM AEKPGAPLAD VLACMMQIHV NTPYLLNHAL
ERLLRGHGHA ASDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNSIA
PSLILFNEHD DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR
