1I1D

CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004343	molecular_function	glucosamine 6-phosphate N-acetyltransferase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0004343	molecular_function	glucosamine 6-phosphate N-acetyltransferase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0004343	molecular_function	glucosamine 6-phosphate N-acetyltransferase activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0004343	molecular_function	glucosamine 6-phosphate N-acetyltransferase activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11278591","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11278591","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I12","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	131
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ygh

Chain	Residue	Details
A	HIS96

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ygh

Chain	Residue	Details
B	HIS96

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ygh

Chain	Residue	Details
C	HIS96

---

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ygh

Chain	Residue	Details
D	HIS96

---