Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003998 | molecular_function | acylphosphatase activity |
A | 0006796 | biological_process | phosphate-containing compound metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
Functional Information from PROSITE/UniProt
site_id | PS00150 |
Number of Residues | 11 |
Details | ACYLPHOSPHATASE_1 Acylphosphatase signature 1. IfGkVQGVfFR |
Chain | Residue | Details |
A | ILE14-ARG24 | |
site_id | PS00151 |
Number of Residues | 17 |
Details | ACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVQNtdrGtVqgqlqG |
Chain | Residue | Details |
A | GLY38-GLY54 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 90 |
Details | Domain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"3026468","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2acy |
Chain | Residue | Details |
A | ARG24 | |
A | ASN42 | |