ID   FOLM_CITK8              Reviewed;         240 AA.
AC   A8AGY5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   24-JAN-2024, entry version 80.
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=CKO_01615;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABV12747.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV12747.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130355.1; NC_009792.1.
DR   AlphaFoldDB; A8AGY5; -.
DR   SMR; A8AGY5; -.
DR   STRING; 290338.CKO_01615; -.
DR   GeneID; 45135664; -.
DR   KEGG; cko:CKO_01615; -.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OrthoDB; 9793499at2; -.
DR   Proteomes; UP000008148; 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   CDD; cd05357; PR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43639:SF6; DIHYDROMONAPTERIN REDUCTASE; 1.
DR   PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_0000339388"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   240 AA;  26280 MW;  A4DDBE321AD47257 CRC64;
     MGKNQPLPIL ITGGGRRIGL AIAWHFLNQK QPVIVSYRTH YPAIDGLTQA GALCIQADFS
     TDDGVLAFAE KIKTHTPGLR AILHNASAWM AEAPGTPLSD VLACMMQIHV NTPYLLNHAL
     ERLLRGHGHA ATDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNAIA
     PSLILFNEND DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FAVDGGRHLR
//