5VMK

Crystal structure of a bifunctional GlmU UDP-N-acetylglucosamine diphosphorylase/glucosamine-1- phosphate N-acetyltransferase from Acinetobacter baumannii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000902	biological_process	cell morphogenesis
A	0003824	molecular_function	catalytic activity
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008360	biological_process	regulation of cell shape
A	0009245	biological_process	lipid A biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization
B	0000287	molecular_function	magnesium ion binding
B	0000902	biological_process	cell morphogenesis
B	0003824	molecular_function	catalytic activity
B	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0008360	biological_process	regulation of cell shape
B	0009245	biological_process	lipid A biosynthetic process
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
C	0000287	molecular_function	magnesium ion binding
C	0000902	biological_process	cell morphogenesis
C	0003824	molecular_function	catalytic activity
C	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
C	0008360	biological_process	regulation of cell shape
C	0009245	biological_process	lipid A biosynthetic process
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
C	0046872	molecular_function	metal ion binding
C	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CIT A 501

Chain	Residue
A	ARG330
A	LYS348
A	TYR363
A	ASN383
A	TYR384
A	LYS389
C	ASN359
C	HIS360
C	ASN374

---

site_id	AC2
Number of Residues	6
Details	binding site for residue PO4 A 502

Chain	Residue
A	GLY11
A	LYS12
A	GLY13
A	ARG15
A	LYS22
A	ASN224

---

site_id	AC3
Number of Residues	8
Details	binding site for residue CIT B 501

Chain	Residue
A	ASN359
A	HIS360
B	ARG330
B	LYS348
B	TYR363
B	ASN383
B	TYR384
B	LYS389

---

site_id	AC4
Number of Residues	9
Details	binding site for residue PG4 B 502

Chain	Residue
A	ALA252
A	ARG270
A	ILE271
A	ASP272
A	GLU288
B	ALA28
B	GLY29
B	GLU233
B	ARG260

---

site_id	AC5
Number of Residues	10
Details	binding site for residue PG4 C 501

Chain	Residue
A	PRO26
A	ALA28
A	GLY29
A	GLU233
C	ALA252
C	ARG270
C	ILE271
C	GLU288
C	ILE289
C	HOH667

---

site_id	AC6
Number of Residues	10
Details	binding site for residue CIT C 502

Chain	Residue
B	ASN359
B	HIS360
B	ASN374
C	ARG330
C	LYS348
C	TYR363
C	ASN383
C	TYR384
C	LYS389
C	HOH640

---

site_id	AC7
Number of Residues	8
Details	binding site for residue PG4 C 503

Chain	Residue
B	ARG270
B	GLU288
C	ALA28
C	GLY29
C	GLU233
C	ARG260
C	HOH635
C	HOH677

---

Functional Information from PROSITE/UniProt

site_id	PS00101
Number of Residues	29
Details	HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGsnSsLvapVtIGngAtVGagSvItkdV

Chain	Residue	Details
A	ILE400-VAL428

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	60
Details	Region: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	65
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---