ID D4F5I2_EDWTA Unreviewed; 240 AA.
AC D4F5I2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dihydromonapterin reductase {ECO:0000256|ARBA:ARBA00039631};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
DE EC=1.5.1.50 {ECO:0000256|ARBA:ARBA00039145};
DE AltName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00042299};
GN ORFNames=EDWATA_02010 {ECO:0000313|EMBL:EFE22976.1};
OS Edwardsiella tarda ATCC 23685.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=500638 {ECO:0000313|EMBL:EFE22976.1, ECO:0000313|Proteomes:UP000003692};
RN [1] {ECO:0000313|EMBL:EFE22976.1, ECO:0000313|Proteomes:UP000003692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23685 {ECO:0000313|EMBL:EFE22976.1,
RC ECO:0000313|Proteomes:UP000003692};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of dihydromonapterin to
CC tetrahydromonapterin. Also has lower activity with dihydrofolate.
CC {ECO:0000256|ARBA:ARBA00037508}.
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:0000256|ARBA:ARBA00001315};
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:0000256|ARBA:ARBA00036516};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FolM subfamily. {ECO:0000256|ARBA:ARBA00038212}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE22976.1}.
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DR EMBL; ADGK01000148; EFE22976.1; -; Genomic_DNA.
DR RefSeq; WP_005285936.1; NZ_GG739633.1.
DR AlphaFoldDB; D4F5I2; -.
DR HOGENOM; CLU_010194_1_3_6; -.
DR Proteomes; UP000003692; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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 One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
SQ SEQUENCE 240 AA; 26121 MW; 17CFFC38C8AB21D6 CRC64;
MDNQPSAPVL ITGGARRVGL ALALALRARA IPVIVAYRSE YPALTQLRQA GVQCLASDFS
TTAGIYDFAR RVQQATPQLR AVIHNASAWQ AESSSVPPEQ TLSAMLQIHV YTPYLLNQLL
EPQLRGQGEA GADIIHITDY VVERGSDGHI AYAASKAALD NMTRSFARKL APEVKVNAIA
PALILFNPED DETYRHKALD KSLMKIAAGE QEIVNAIYFL LNSRFITGRT IGVDGGRPLR
//
