4R7T

Crystal structure of glucosamine-6-phosphate deaminase from Vibrio cholerae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
A	0005737	cellular_component	cytoplasm
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	0016787	molecular_function	hydrolase activity
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0042802	molecular_function	identical protein binding
B	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
B	0005737	cellular_component	cytoplasm
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	0016787	molecular_function	hydrolase activity
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0042802	molecular_function	identical protein binding
C	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
C	0005737	cellular_component	cytoplasm
C	0005975	biological_process	carbohydrate metabolic process
C	0006043	biological_process	glucosamine catabolic process
C	0006044	biological_process	N-acetylglucosamine metabolic process
C	0006046	biological_process	N-acetylglucosamine catabolic process
C	0016787	molecular_function	hydrolase activity
C	0019262	biological_process	N-acetylneuraminate catabolic process
C	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	ILE97
A	HOH414
A	HOH434
A	HOH435
B	ASP112

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 302

Chain	Residue
A	ASN140

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 303

Chain	Residue
C	PRO149
A	TYR254
A	HOH427
C	ASP141

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 300

Chain	Residue
B	ILE97
B	HOH422
B	HOH435
B	HOH451
B	HOH452
C	ASP112

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT B 301

Chain	Residue
B	GLY43
B	THR44

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 300

Chain	Residue
A	ASP112
A	HOH420
C	ILE97
C	HOH434
C	HOH463
C	HOH464

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE125-HIS143

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor; for enolization step => ECO:0000255|HAMAP-Rule:MF_01241

Chain	Residue	Details
A	ASP72
B	ASP72
C	ASP72

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: For ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241

Chain	Residue	Details
A	ASP141
A	GLU148
B	ASP141
B	GLU148
C	ASP141
C	GLU148

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	ACT_SITE: Proton acceptor; for ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241

Chain	Residue	Details
A	HIS143
B	HIS143
C	HIS143

---

site_id	SWS_FT_FI4
Number of Residues	15
Details	SITE: Part of the allosteric site => ECO:0000255|HAMAP-Rule:MF_01241

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

---