7ZD7

Crystal structure of the R24E/E352T double mutant of S-adenosyl-L-homocysteine hydrolase from Synechocystis sp. PCC 6803 cocrystallized with adenosine in the presence of Rb+ cations

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033353	biological_process	S-adenosylmethionine cycle
A	0071269	biological_process	L-homocysteine biosynthetic process
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006730	biological_process	one-carbon metabolic process
C	0016787	molecular_function	hydrolase activity
C	0033353	biological_process	S-adenosylmethionine cycle
C	0071269	biological_process	L-homocysteine biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00738
Number of Residues	15
Details	ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. ASNpLSTQDdVAACL

Chain	Residue	Details
A	ALA81-LEU95

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site_id	PS00739
Number of Residues	17
Details	ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKtivVaGYGwCGKGv.A

Chain	Residue	Details
A	GLY214-ALA230

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563

Chain	Residue	Details
A	THR60
A	ASN279
A	SER300
A	ASN347
C	THR60
C	ASP132
C	GLU157
C	THR158
C	LYS187
C	ASP191
C	ASN192
A	ASP132
C	GLY221
C	GLU244
C	ASN279
C	SER300
C	ASN347
A	GLU157
A	THR158
A	LYS187
A	ASP191
A	ASN192
A	GLY221
A	GLU244

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