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, using agmatinase
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, using agmatinase
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, using agmatinase
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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00742

Chain	Residue	Details
A	HIS174
B	ASP203
B	ASP291
B	ASP293
C	HIS174
C	ASP199
C	HIS201
C	ASP203
C	ASP291
C	ASP293
A	ASP199
A	HIS201
A	ASP203
A	ASP291
A	ASP293
B	HIS174
B	ASP199
B	HIS201

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