1XFK
1.8A crystal structure of formiminoglutamase from Vibrio cholerae O1 biovar eltor str. N16961
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006547 | biological_process | L-histidine metabolic process |
| A | 0006548 | biological_process | L-histidine catabolic process |
| A | 0008783 | molecular_function | agmatinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050415 | molecular_function | formimidoylglutamase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. TIDLDvfpAasaPGvsapaarG |
| Chain | Residue | Details |
| A | THR252-GLY273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00737","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| A | GLU300 | |
| A | ASP161 |






