1ECF

ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004044	molecular_function	amidophosphoribosyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0006541	biological_process	glutamine metabolic process
A	0009113	biological_process	purine nucleobase biosynthetic process
A	0016757	molecular_function	glycosyltransferase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000287	molecular_function	magnesium ion binding
B	0004044	molecular_function	amidophosphoribosyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0006541	biological_process	glutamine metabolic process
B	0009113	biological_process	purine nucleobase biosynthetic process
B	0016757	molecular_function	glycosyltransferase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PIN A 505

Chain	Residue
A	PRO302
A	GLU303
A	THR304
A	ASP366
A	ASP367
A	SER368
A	VAL370
A	ARG371
A	GLY372
A	THR373
A	THR374
A	HOH551
A	HOH849

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PIN A 506

Chain	Residue
A	ARG43
A	LEU44
A	ARG45
A	LYS46
A	ARG62
A	HOH810
A	HOH836
A	HOH836
A	HOH982

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PIN A 507

Chain	Residue
A	TYR89
A	TYR89
A	VAL90
A	VAL90
A	ASN91
A	ASN91
A	HOH511
A	HOH511

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PIN B 505

Chain	Residue
A	HOH786
B	GLU303
B	THR304
B	LYS326
B	ASP366
B	ASP367
B	SER368
B	ILE369
B	VAL370
B	ARG371
B	GLY372
B	THR373
B	THR374
B	SER375
B	HOH848
B	HOH910

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PIN B 506

Chain	Residue
B	ARG43
B	LEU44
B	LEU44
B	ARG45
B	LYS46
B	ARG62
B	ARG62
B	GLU84
B	HOH770
B	HOH884
B	HOH943

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PIN B 507

Chain	Residue
B	TYR89
B	TYR89
B	VAL90
B	VAL90
B	ASN91
B	ASN91
B	SER92
B	HOH555

---

site_id	NTA
Number of Residues	1
Details	NTN TYPE GLUTAMINE AMIDOTRANSFERASE CATALYTIC RESIDUE. THIS SITE BELONGS TO THE NTN SUPERFAMILY, WHICH ARE THOUGHT TO UTILIZE THE ALPHA-AMINO GROUP OF THE N-TERMINAL RESIDUE AS A PROTON DONOR , AND THE SIDE CHAIN OF THIS RESIDUE AS A NUCLEOPHILE IN CATALYSIS OF A HYDROLYTIC REACTION.

Chain	Residue
A	CYS1

---

site_id	NTB
Number of Residues	1
Details	NTN TYPE GLUTAMINE AMIDOTRANSFERASE CATALYTIC RESIDUE. THIS SITE BELONGS TO THE NTN SUPERFAMILY, WHICH ARE THOUGHT TO UTILIZE THE ALPHA-AMINO GROUP OF THE N-TERMINAL RESIDUE AS A PROTON DONOR , AND THE SIDE CHAIN OF THIS RESIDUE AS A NUCLEOPHILE IN CATALYSIS OF A HYDROLYTIC REACTION.

Chain	Residue
B	CYS1

---

site_id	PRA
Number of Residues	13
Details	PRPP BINDING MOTIF, IDENTIFIED BY SEQUENCE SIMILARITY AMONG MEMBERS OF THE PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES.

Chain	Residue
A	ILE369
A	VAL370
A	ARG371
A	GLY372
A	THR373
A	THR374
A	VAL362
A	LEU363
A	LEU364
A	VAL365
A	ASP366
A	ASP367
A	SER368

---

site_id	PRB
Number of Residues	13
Details	PRPP BINDING MOTIF, IDENTIFIED BY SEQUENCE SIMILARITY AMONG MEMBERS OF THE PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES.

Chain	Residue
B	VAL362
B	LEU363
B	LEU364
B	VAL365
B	ASP366
B	ASP367
B	SER368
B	ILE369
B	VAL370
B	ARG371
B	GLY372
B	THR373
B	THR374

---

Functional Information from PROSITE/UniProt

site_id	PS00103
Number of Residues	13
Details	PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLLVDDSIVRGtT

Chain	Residue	Details
A	VAL362-THR374

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784

Chain	Residue	Details
A	GLY2
B	GLY2

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931

Chain	Residue	Details
A	SER305
A	ASP367
A	SER368
B	SER305
B	ASP367
B	SER368

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 9514258, 9914248

Chain	Residue	Details
A	CYS1
A	ASN101
A	GLY102

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 214

Chain	Residue	Details
A	GLY2	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLN28	activator, electrostatic stabiliser, hydrogen bond acceptor
A	GLY102	electrostatic stabiliser, hydrogen bond donor
A	ASN103	electrostatic stabiliser, hydrogen bond donor
A	PHE259	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 214

Chain	Residue	Details
B	GLY2	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
B	GLN28	activator, electrostatic stabiliser, hydrogen bond acceptor
B	GLY102	electrostatic stabiliser, hydrogen bond donor
B	ASN103	electrostatic stabiliser, hydrogen bond donor
B	PHE259	electrostatic stabiliser, hydrogen bond donor

---