EzCatDB: D00299
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DB codeD00299
CATH domainDomain 13.30.1330.10 : 60s Ribosomal Protein L30; ChainCatalytic domain
Domain 23.90.650.10 : Phosphoribosyl-aminoimidazole Synthetase; Chain A, domain 2Catalytic domain
E.C.6.3.3.1


Enzyme Name
UniProtKBKEGG

P08178
Protein namePhosphoribosylformylglycinamidine cyclo-ligasephosphoribosylformylglycinamidine cyclo-ligase
phosphoribosylaminoimidazole synthetase
AIR synthetase
5'-aminoimidazole ribonucleotide synthetase
2-(formamido)-1-N-(5-phosphoribosyl)acetamidine cyclo-ligase(ADP-forming)
SynonymsEC 6.3.3.1
AIRS
Phosphoribosyl-aminoimidazole synthetase
AIR synthase
RefSeqNP_416994.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490727.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00586 (AIRS)
PF02769 (AIRS_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism

UniProtKB:Accession NumberP08178
Entry namePUR5_ECOLI
ActivityATP + 2-(formamido)-N(1)-(5-phospho-D- ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- ribosyl)imidazole.
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00002C04640C00008C00009C03373
CompoundMagnesiumATP2-(Formamido)-N1-(5'-phosphoribosyl)acetamidineADPOrthophosphate1-(5'-Phosphoribosyl)-5-aminoimidazole
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamine group,carbohydrate,imine group,phosphate group/phosphate ionamine group,nucleotidephosphate group/phosphate ionamine group,nucleotide
ChEBI18420
15422

16761
26078

PubChem888
5957
9552078
5462266
440417
6022
22486802
1004
161500
              
1cliA01UnboundUnboundUnboundUnboundUnboundUnbound
1cliB01UnboundUnboundUnboundUnboundUnboundUnbound
1cliC01UnboundUnboundUnboundUnboundUnboundUnbound
1cliD01UnboundUnboundUnboundUnboundUnboundUnbound
1cliA02UnboundUnboundUnboundUnboundAnalogue:SO4Unbound
1cliB02UnboundUnboundUnboundUnboundAnalogue:SO4Unbound
1cliC02UnboundUnboundUnboundUnboundAnalogue:SO4Unbound
1cliD02UnboundUnboundUnboundUnboundAnalogue:SO4Unbound

Active-site residues
resource
literature [4]
pdbCatalytic residuesCofactor-binding residues
          
1cliA01 
ASP   94;GLU  141(magnesium ion)
1cliB01 
ASP 1094;GLU 1141(magnesium ion)
1cliC01 
ASP 2094;GLU 2141(magnesium ion)
1cliD01 
ASP 3094;GLU 3141(magnesium ion)
1cliA02HIS  247;THR  249;ARG  259
 
1cliB02HIS 1247;THR 1249;ARG 1259
 
1cliC02HIS 2247;THR 2249;ARG 2259
 
1cliD02HIS 3247;THR 3249;ARG 3259
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme I, p.4364
[2]Scheme Ip.4369
[4]Fig.1, p.1159-1161
[5]Fig.1

references
[1]
PubMed ID3756144
JournalBiochemistry
Year1986
Volume25
Pages4356-65
AuthorsSchrimsher JL, Schendel FJ, Stubbe J
TitleIsolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase.
[2]
PubMed ID3530323
JournalBiochemistry
Year1986
Volume25
Pages4366-71
AuthorsSchrimsher JL, Schendel FJ, Stubbe J, Smith JM
TitlePurification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli.
[3]
PubMed ID8299947
JournalGene
Year1993
Volume137
Pages195-202
AuthorsKan JL, Jannatipour M, Taylor SM, Moran RG
TitleMouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID99451262
PubMed ID10508786
JournalStructure Fold Des
Year1999
Volume7
Pages1155-66
AuthorsLi C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE
TitleX-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.
Related PDB1cli
Related UniProtKBP08178
[5]
PubMed ID15301531
JournalBiochemistry
Year2004
Volume43
Pages10328-42
AuthorsAnand R, Hoskins AA, Stubbe J, Ealick SE
TitleDomain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.

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.

createdupdated
2004-09-162009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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