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 CCATGACATTTAAGAGAAGAATTACAGCATTTTAAAGAAACAACATTAGGGCAAACAATT TTATTTGGTCGGTTGACTTATGAAGGAATTGGACGACCATTACCAAAACGAAAAACATTA GTTTTAACAAGACAGCTTGATTATCAAATTAAGCATCCAGATGTGGAAGTAGTAACTGAT TTAACAGCAATTATTAATTTTTATCATCAAAATCCAACCGAAGATATTTATATTTGTGGG GGAAAAAAAATTTATGAGGCAACATTACCATATGCTGATGAATTAATTACTAGTCTTATT AAAGGAAAATACCAAGGCGATACTTATTTTCCTTCGTTTGATTTAAACCAATTTACTTTA ACTAAATTAAACGAATATCAACAATTTGTAATAAAATATTATAAGAGAAAGGAACAAAGT TAA >protein sequence VLTRQLDYQIKHPDVEVVTDLTAIINFYHQNPTEDIYICGGKKIYEATLPYADELITSLI KGKYQGDTYFPSFDLNQFTLTKLNEYQQFVIKYYKRKEQS |
© Fisunov Lab of Proteomics, 2016.