2VHL

The Three-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis

Replaces: 1UN7

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0006040	biological_process	amino sugar metabolic process
A	0006044	biological_process	N-acetylglucosamine metabolic process
A	0006046	biological_process	N-acetylglucosamine catabolic process
A	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0005506	molecular_function	iron ion binding
B	0006040	biological_process	amino sugar metabolic process
B	0006044	biological_process	N-acetylglucosamine metabolic process
B	0006046	biological_process	N-acetylglucosamine catabolic process
B	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:14557261

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:14557261, ECO:0007744\|PDB:2VHL

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P0AF18