1FS5

A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006043	biological_process	glucosamine catabolic process
A	0006044	biological_process	N-acetylglucosamine metabolic process
A	0006046	biological_process	N-acetylglucosamine catabolic process
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008152	biological_process	metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006043	biological_process	glucosamine catabolic process
B	0006044	biological_process	N-acetylglucosamine metabolic process
B	0006046	biological_process	N-acetylglucosamine catabolic process
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0008152	biological_process	metabolic process
B	0016787	molecular_function	hydrolase activity
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS01161
Number of Residues	19
Details	GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IrsyGkIhLfMgGVGnDGH

Chain	Residue	Details
A	ILE125-HIS143

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor; for enolization step => ECO:0000269|PubMed:11513596

Chain	Residue	Details
A	ASP72
B	ASP72

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: For ring-opening step => ECO:0000269|PubMed:11513596

Chain	Residue	Details
A	ASP141
A	GLU148
B	ASP141
B	GLU148

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton acceptor; for ring-opening step => ECO:0000269|PubMed:11513596

Chain	Residue	Details
A	HIS143
B	HIS143

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site_id	SWS_FT_FI4
Number of Residues	10
Details	SITE: Part of the allosteric site

Chain	Residue	Details
A	SER151
B	TYR254
A	ARG158
A	LYS160
A	THR161
A	TYR254
B	SER151
B	ARG158
B	LYS160
B	THR161

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 60

Chain	Residue	Details
A	ASP72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP141	activator, hydrogen bond acceptor
A	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLU148	activator, hydrogen bond acceptor

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 60

Chain	Residue	Details
B	ASP72	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP141	activator, hydrogen bond acceptor
B	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLU148	activator, hydrogen bond acceptor

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