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, using agmatinase |
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 | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00737 |
Chain | Residue | Details |
A | HIS127 | |
A | ASP157 | |
A | HIS159 | |
A | ASP161 | |
A | ASP254 | |
A | ASP256 |
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 |