SPM_005815


  Uniprot: A0A037UNS5
Description: dihydrofolate reductase
EC number: 1.5.1.3
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. {ECO:0000256|PIRNR:PIRNR000194}.
Cofactor: 
Enzyme regulation: 
Function [CC]: FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.
Pathway: PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. {ECO:0000256|PIRNR:PIRNR000194}.
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): 
Gene names (synonym): 
Mass: 18,909
Subunit structure [CC]: 
Gene ontology (GO): dihydrofolate reductase activity [GO:0004146]; NADP binding [GO:0050661]; glycine biosynthetic process [GO:0006545]; nucleotide biosynthetic process [GO:0009165]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate biosynthetic process [GO:0046654]
Gene ontology IDs: GO:0004146; GO:0006545; GO:0006730; GO:0009165; GO:0046654; GO:0050661
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the dihydrofolate reductase family. {ECO:0000256|PIRNR:PIRNR000194}.
Protein families: Dihydrofolate reductase family
Coiled coil: 
Domain [FT]: DOMAIN 1 160 DHFR (dihydrofolate reductase). {ECO:0000259|PROSITE:PS51330}.
Motif: 
Region: 
EMBL: AGBZ02000004
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92243
UniPathway: 
CDD: 
Gene3D: cd00209
HAMAP: 3.40.430.10
InterPro: 
PANTHER: IPR012259;IPR024072;IPR017925;IPR001796
PIRSF: 
PRINTS: PIRSF000194
PROSITE: PR00070
Pfam: PS00075;PS51330
ProDom: PF00186
SMART: 
SUPFAM: 
TIGRFAMs: SSF53597
227550-228033(+)

>nucleotide sequence
ATGATTAAGTTATTATGAGCAATGGATGAAAATAATTTAATTGGTCAAAATAACCAATTA
CCATGACATTTAAGAGAAGAATTACAGCATTTTAAAGAAACAACATTAGGGCAAACAATT
TTATTTGGTCGGTTGACTTATGAAGGAATTGGACGACCATTACCAAAACGAAAAACATTA
GTTTTAACAAGACAGCTTGATTATCAAATTAAGCATCCAGATGTGGAAGTAGTAACTGAT
TTAACAGCAATTATTAATTTTTATCATCAAAATCCAACCGAAGATATTTATATTTGTGGG
GGAAAAAAAATTTATGAGGCAACATTACCATATGCTGATGAATTAATTACTAGTCTTATT
AAAGGAAAATACCAAGGCGATACTTATTTTCCTTCGTTTGATTTAAACCAATTTACTTTA
ACTAAATTAAACGAATATCAACAATTTGTAATAAAATATTATAAGAGAAAGGAACAAAGT
TAA


>protein sequence
MIKLLWAMDENNLIGQNNQLPWHLREELQHFKETTLGQTILFGRLTYEGIGRPLPKRKTL
VLTRQLDYQIKHPDVEVVTDLTAIINFYHQNPTEDIYICGGKKIYEATLPYADELITSLI
KGKYQGDTYFPSFDLNQFTLTKLNEYQQFVIKYYKRKEQS






















© Fisunov Lab of Proteomics, 2016.