EzCatDB: D00131

DB codeD00131
CATH domainDomain 13.40.50.2020Catalytic domain
Domain 23.40.50.2020Catalytic domain
E.C.2.7.6.1

CATH domainRelated DB codes (homologues)
3.40.50.2020S00288,S00289,S00287

Enzyme Name
Swiss-protKEGG

P14193
Protein nameRibose-phosphate pyrophosphokinaseribose-phosphate diphosphokinase
ribose-phosphate pyrophosphokinase
PRPP synthetase
phosphoribosylpyrophosphate synthetase
PPRibP synthetase
PP-ribose P synthetase
5-phosphoribosyl-1-pyrophosphate synthetase
5-phosphoribose pyrophosphorylase
5-phosphoribosyl-alpha-1-pyrophosphate synthetase
phosphoribosyl-diphosphate synthetase
phosphoribosylpyrophosphate synthase
pyrophosphoribosylphosphate synthetase
ribophosphate pyrophosphokinase
ribose-5-phosphate pyrophosphokinase
SynonymsRPPK
EC 2.7.6.1
Phosphoribosyl pyrophosphate synthetase
P-Rib-PP synthetase
PRPP synthetase

KEGG pathways
MAP codePathways
MAP00030Pentose phosphate pathway
MAP00230Purine metabolism

Swiss-prot:Accession NumberP14193
Entry nameKPRS_BACSU
ActivityATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate.
SubunitHomohexamer.
Subcellular locationCytoplasm (By similarity).
CofactorBinds 1 magnesium ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00305C00002C00131C00117C00020C00360C00119
CompoundMagnesiumATPdATPD-Ribose 5-phosphateAMPdAMP5-Phospho-alpha-D-ribose 1-diphosphate
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamine group,nucleotidecarbohydrate,phosphate group/phosphate ionamine group,nucleotideamine group,nucleotidecarbohydrate,phosphate group/phosphate ion
1dkrA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dkrB01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dkuA01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dkuB01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ibsA01Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnbound
1ibsB01Analogue:_CDUnboundUnboundUnboundUnboundUnboundUnbound
1dkrA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dkrB02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dkuA02UnboundAnalogue:AP2UnboundUnboundAnalogue:ABMUnboundUnbound
1dkuB02UnboundAnalogue:AP2UnboundUnboundAnalogue:ABMUnboundUnbound
1ibsA02Analogue:_CDUnboundUnboundUnboundAnalogue:ABMUnboundUnbound
1ibsB02Analogue:_CDUnboundUnboundUnboundAnalogue:ABMUnboundUnbound

Active-site residues
resource
Swiss-prot
pdbCatalytic residuesCofactor-binding residues
1dkrA01LYS 197

1dkrB01LYS 197

1dkuA01LYS 197

1dkuB01LYS 197

1ibsA01LYS 197

1ibsB01LYS 197

1dkrA02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkrB02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkuA02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkuB02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1ibsA02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1ibsB02ARG 101
ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]p.305-306
[8]p.737
[10]p.2319-2320
[11]p.277

references
[1]
PubMed ID6330252
JournalJ Lab Clin Med
Year1984
Volume104
Pages96-109
AuthorsItkin P, Woo S, Becker MA
TitleHuman phosphoribosylpyrophosphate synthetase: radioimmunochemical quantitation in erythrocytes and fibroblasts.
[2]
PubMed ID2414323
JournalJ Clin Invest
Year1985
Volume76
Pages1657-64
AuthorsLosman MJ, Rimon D, Kim M, Becker MA
TitleSelective expression of phosphoribosylpyrophosphate synthetase superactivity in human lymphoblast lines.
[3]
PubMed ID3017368
JournalArthritis Rheum
Year1986
Volume29
Pages880-8
AuthorsBecker MA, Losman MJ, Rosenberg AL, Mehlman I, Levinson DJ, Holmes EW
TitlePhosphoribosylpyrophosphate synthetase superactivity. A study of five patients with catalytic defects in the enzyme.
[4]
PubMed ID2546925
JournalJ Biochem (Tokyo)
Year1989
Volume105
Pages736-41
AuthorsKita K, Otsuki T, Ishizuka T, Tatibana M
TitleRat liver phosphoribosyl pyrophosphate synthetase: existence of the purified enzyme as heterogeneous aggregates and identification of the catalytic subunit.
[5]
PubMed ID8820490
JournalProteins
Year1996
Volume24
Pages238-46
AuthorsBentsen AK, Larsen TA, Kadziola A, Larsen S, Harlow KW
TitleOverexpression of Bacillus subtilis phosphoribosylpyrophosphate synthetase and crystallization and preliminary X-ray characterization of the free enzyme and its substrate-effector complexes.
Related PDB1kdr
[6]
PubMed ID9348095
JournalJ Biochem (Tokyo)
Year1997
Volume122
Pages635-40
AuthorsSonoda T, Kita K, Ishijima S, Ishizuka T, Ahmad I, Tatibana M
TitleKinetic and regulatory properties of rat liver phosphoribosylpyrophosphate synthetase complex are partly distinct from those of isolated recombinant component catalytic subunits.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID20207047
PubMed ID10742175
JournalNat Struct Biol
Year2000
Volume7
Pages303-8
AuthorsEriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S
TitleStructural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
Related PDB1dkr,1dku
Related Swiss-protP14193
[8]
PubMed ID11751055
JournalCurr Opin Struct Biol
Year2001
Volume11
Pages733-9
AuthorsSinha SC, Smith JL
TitleThe PRT protein family.
[9]
PubMed ID11278632
JournalJ Biol Chem
Year2001
Volume276
Pages17851-6
AuthorsKrath BN, Hove-Jensen B
TitleClass II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity.
[10]
PubMed ID11604537
JournalProtein Sci
Year2001
Volume10
Pages2317-24
AuthorsKrath BN, Hove-Jensen B
TitleImplications of secondary structure prediction and amino acid sequence comparison of class I and class II phosphoribosyl diphosphate synthases on catalysis, regulation, and quaternary structure.
[11]
PubMed ID11790837
JournalProtein Sci
Year2002
Volume11
Pages271-9
AuthorsEriksen TA, Kadziola A, Larsen S
TitleBinding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis.


createdupdated
2004-03-182009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
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)

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