DB code: D00131

CATH domain 3.40.50.2020 : Rossmann fold Catalytic domain
3.40.50.2020 : Rossmann fold Catalytic domain
E.C. 2.7.6.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.2020 : Rossmann fold S00288 S00289 S00287

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P14193 Ribose-phosphate pyrophosphokinase
RPPK
EC 2.7.6.1
Phosphoribosyl pyrophosphate synthetase
P-Rib-PP synthetase
PRPP synthetase
NP_387932.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PF00156 (Pribosyltran)
[Graphical View]

KEGG enzyme name
ribose-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P14193 KPRS_BACSU ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate. Homohexamer. Cytoplasm (By similarity). Binds 1 magnesium ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00030 Pentose phosphate pathway
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C00131 C00117 C00020 C00360 C00119
E.C.
Compound Magnesium ATP dATP D-Ribose 5-phosphate AMP dAMP 5-Phospho-alpha-D-ribose 1-diphosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,nucleotide carbohydrate,phosphate group/phosphate ion amine group,nucleotide amine group,nucleotide carbohydrate,phosphate group/phosphate ion
ChEBI 18420
15422
16284
52742
16027
17713
17111
PubChem 888
5957
15993
439167
6083
12599
7339
1dkrA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dkrB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dkuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dkuB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ibsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound
1ibsB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CD Unbound Unbound Unbound Unbound Unbound Unbound
1dkrA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dkrB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dkuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:AP2 Unbound Unbound Analogue:ABM Unbound Unbound
1dkuB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:AP2 Unbound Unbound Analogue:ABM Unbound Unbound
1ibsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CD Unbound Unbound Unbound Analogue:ABM Unbound Unbound
1ibsB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_CD Unbound Unbound Unbound Analogue:ABM Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dkrA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1dkrB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1dkuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1dkuB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1ibsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1ibsB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 197
1dkrA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkrB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1dkuB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1ibsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)
1ibsB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 101 ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
p.305-306
[8]
p.737
[10]
p.2319-2320
[11]
p.277

References
[1]
Resource
Comments
Medline ID
PubMed ID 6330252
Journal J Lab Clin Med
Year 1984
Volume 104
Pages 96-109
Authors Itkin P, Woo S, Becker MA
Title Human phosphoribosylpyrophosphate synthetase: radioimmunochemical quantitation in erythrocytes and fibroblasts.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2414323
Journal J Clin Invest
Year 1985
Volume 76
Pages 1657-64
Authors Losman MJ, Rimon D, Kim M, Becker MA
Title Selective expression of phosphoribosylpyrophosphate synthetase superactivity in human lymphoblast lines.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3017368
Journal Arthritis Rheum
Year 1986
Volume 29
Pages 880-8
Authors Becker MA, Losman MJ, Rosenberg AL, Mehlman I, Levinson DJ, Holmes EW
Title Phosphoribosylpyrophosphate synthetase superactivity. A study of five patients with catalytic defects in the enzyme.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2546925
Journal J Biochem (Tokyo)
Year 1989
Volume 105
Pages 736-41
Authors Kita K, Otsuki T, Ishizuka T, Tatibana M
Title Rat liver phosphoribosyl pyrophosphate synthetase: existence of the purified enzyme as heterogeneous aggregates and identification of the catalytic subunit.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8820490
Journal Proteins
Year 1996
Volume 24
Pages 238-46
Authors Bentsen AK, Larsen TA, Kadziola A, Larsen S, Harlow KW
Title Overexpression of Bacillus subtilis phosphoribosylpyrophosphate synthetase and crystallization and preliminary X-ray characterization of the free enzyme and its substrate-effector complexes.
Related PDB 1kdr
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9348095
Journal J Biochem (Tokyo)
Year 1997
Volume 122
Pages 635-40
Authors Sonoda T, Kita K, Ishijima S, Ishizuka T, Ahmad I, Tatibana M
Title Kinetic and regulatory properties of rat liver phosphoribosylpyrophosphate synthetase complex are partly distinct from those of isolated recombinant component catalytic subunits.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 20207047
PubMed ID 10742175
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 303-8
Authors Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S
Title Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
Related PDB 1dkr 1dku
Related UniProtKB P14193
[8]
Resource
Comments
Medline ID
PubMed ID 11751055
Journal Curr Opin Struct Biol
Year 2001
Volume 11
Pages 733-9
Authors Sinha SC, Smith JL
Title The PRT protein family.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11278632
Journal J Biol Chem
Year 2001
Volume 276
Pages 17851-6
Authors Krath BN, Hove-Jensen B
Title Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11604537
Journal Protein Sci
Year 2001
Volume 10
Pages 2317-24
Authors Krath BN, Hove-Jensen B
Title Implications of secondary structure prediction and amino acid sequence comparison of class I and class II phosphoribosyl diphosphate synthases on catalysis, regulation, and quaternary structure.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11790837
Journal Protein Sci
Year 2002
Volume 11
Pages 271-9
Authors Eriksen TA, Kadziola A, Larsen S
Title Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-18 2009-02-26