7OI1

Crystal structure of Synechocystis sp PCC6803 guanidinium hydrolase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
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	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0008783	molecular_function	agmatinase activity
B	0016787	molecular_function	hydrolase activity
B	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0008783	molecular_function	agmatinase activity
C	0016787	molecular_function	hydrolase activity
C	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
C	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS01053
Number of Residues	22
Details	ARGINASE_1 Arginase family signature. SFDIDcidAgfvPGtgwpepgG

Chain	Residue	Details
A	SER289-GLY310

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35264792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OI1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---