DB code: D00299

CATH domain 3.30.1330.10 : 60s Ribosomal Protein L30; Chain Catalytic domain
3.90.650.10 : Phosphoribosyl-aminoimidazole Synthetase; Chain A, domain 2 Catalytic domain
E.C. 6.3.3.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P08178 Phosphoribosylformylglycinamidine cyclo-ligase
EC 6.3.3.1
AIRS
Phosphoribosyl-aminoimidazole synthetase
AIR synthase
NP_416994.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490727.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00586 (AIRS)
PF02769 (AIRS_C)
[Graphical View]

KEGG enzyme name
phosphoribosylformylglycinamidine cyclo-ligase
phosphoribosylaminoimidazole synthetase
AIR synthetase
5'-aminoimidazole ribonucleotide synthetase
2-(formamido)-1-N-(5-phosphoribosyl)acetamidine cyclo-ligase(ADP-forming)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08178 PUR5_ECOLI ATP + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- ribosyl)imidazole. Homodimer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C04640 C00008 C00009 C03373
E.C.
Compound Magnesium ATP 2-(Formamido)-N1-(5'-phosphoribosyl)acetamidine ADP Orthophosphate 1-(5'-Phosphoribosyl)-5-aminoimidazole
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,carbohydrate,imine group,phosphate group/phosphate ion amine group,nucleotide phosphate group/phosphate ion amine group,nucleotide
ChEBI 18420
15422
16761
26078
PubChem 888
5957
440417
5462266
9552078
6022
1004
22486802
161500
1cliA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1cliB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1cliC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1cliD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1cliA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:SO4 Unbound
1cliB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:SO4 Unbound
1cliC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:SO4 Unbound
1cliD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:SO4 Unbound

Reference for Active-site residues
resource references E.C.
literature [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cliA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 94;GLU 141(magnesium ion)
1cliB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 1094;GLU 1141(magnesium ion)
1cliC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 2094;GLU 2141(magnesium ion)
1cliD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 3094;GLU 3141(magnesium ion)
1cliA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 247;THR 249;ARG 259
1cliB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 1247;THR 1249;ARG 1259
1cliC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 2247;THR 2249;ARG 2259
1cliD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 3247;THR 3249;ARG 3259

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Scheme I, p.4364
[2]
Scheme I p.4369
[4]
Fig.1, p.1159-1161
[5]
Fig.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 3756144
Journal Biochemistry
Year 1986
Volume 25
Pages 4356-65
Authors Schrimsher JL, Schendel FJ, Stubbe J
Title Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3530323
Journal Biochemistry
Year 1986
Volume 25
Pages 4366-71
Authors Schrimsher JL, Schendel FJ, Stubbe J, Smith JM
Title Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8299947
Journal Gene
Year 1993
Volume 137
Pages 195-202
Authors Kan JL, Jannatipour M, Taylor SM, Moran RG
Title Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 99451262
PubMed ID 10508786
Journal Structure Fold Des
Year 1999
Volume 7
Pages 1155-66
Authors Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE
Title X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.
Related PDB 1cli
Related UniProtKB P08178
[5]
Resource
Comments
Medline ID
PubMed ID 15301531
Journal Biochemistry
Year 2004
Volume 43
Pages 10328-42
Authors Anand R, Hoskins AA, Stubbe J, Ealick SE
Title Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.
Related PDB
Related UniProtKB

Comments
This enzyme catalyze three different reactions:
(1) Phosphoryl transfer from ATP to carbonyl oxygen of the substrate, FGAM (C04640), resulting in the formation of iminophosphate intermediate.
(2) Imine group transfer from the iminophosphate intermediate to amine group (N1 atom).
(3) Isomerization of imine group to amine group.
However, the detailed catalytic mechanism has not been proposed yet.
According to the literature [4], putative catalytic residues are proposed: Asp94, His247, Thr249 & Arg259. Asp94 and Glu141 can be involved in magnesium binding.

Created Updated
2004-09-16 2009-02-26