FOLM_KLEP7
ID FOLM_KLEP7 Reviewed; 240 AA.
AC A6T8N3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=KPN78578_14930; ORFNames=KPN_01523;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR76954.1; -; Genomic_DNA.
DR RefSeq; WP_004176334.1; NC_009648.1.
DR AlphaFoldDB; A6T8N3; -.
DR SMR; A6T8N3; -.
DR STRING; 272620.KPN_01523; -.
DR EnsemblBacteria; ABR76954; ABR76954; KPN_01523.
DR KEGG; kpn:KPN_01523; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; QIHVHAP; -.
DR Proteomes; UP000000265; 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_0000339398"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ SEQUENCE 240 AA; 26418 MW; ADDC4B3252A4DC75 CRC64;
MAEQQPRPIL ITGAGRRIGL ALAHHFLQQR QPVIVSYRTP YPAIDGLREA GALCLQADFS
SDDGILTFAE AVKSHTDGLR AIIHNASDWM AEKPGVPLST VINRMMQIHV HAPYLLNHAL
EALLRGHGHA ASDIIHITDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNAIA
PSLIMFNEGD DEAYRQQALD KSLMKIAPGE KEISDLIDYL FTSRYVTGRS FAVDGGRPLR