B4DPT6 · B4DPT6_HUMAN
- ProteinSugar phosphate phosphatase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids322 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism. Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Possibly methylates PCNA, suggesting it is involved in the DNA damage response.
Catalytic activity
- L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
- beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate
- beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone
Cofactor
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | fructose 6-phosphate aldolase activity | |
Molecular Function | fructose-1-phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein-glutamate O-methyltransferase activity | |
Biological Process | methylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSugar phosphate phosphatase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionB4DPT6
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Organism-specific databases
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-300 | Damage-control phosphatase ARMT1-like metal-binding | ||||
Sequence: MYRRIHEAIIQSPLIDYFDVFKESKEQNFYGSQESIIALCTHLQQLIRTIEDLDENQLKDEFFKLLQISLWGNKCDLSLSGGESSSQNTNVLNSLEDLKPFILLNDMEHLWSLLSNCKKTREKASATRVYIVLDNSGFELVTDLILADFLLSSELATEVHFYGKTIPWFVSDTTIHDFNWLIEQVKHSNHKWMSKCGTDWEEYIKMGKWVYHNHIFWTLPHEYCAMPQVAPDLYAELQKAHLILFKGDLNYRKLTGDRKWEFSVPFHQALNGFHPAPLCTIRALKAEIQVGLQPGQGEQL |
Domain
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)37,370
- Last updated2008-09-23 v1
- Checksum14A7443F22AF76CC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK298490 EMBL· GenBank· DDBJ | BAG60698.1 EMBL· GenBank· DDBJ | mRNA |