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 18420 |
15422 15422 |
16284 16284 |
52742 52742 |
16027 16027 |
17713 17713 |
17111 17111 |
||||||
PubChem |
888 888 |
5957 5957 |
15993 15993 |
439167 439167 |
6083 6083 |
12599 12599 |
7339 7339 |
||||||
1dkrA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkrB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkuA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkuB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ibsA01 | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1ibsB01 | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkrA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkrB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1dkuA02 | Unbound | Analogue:AP2 | Unbound | Unbound | Analogue:ABM | Unbound | Unbound | ||||||
1dkuB02 | Unbound | Analogue:AP2 | Unbound | Unbound | Analogue:ABM | Unbound | Unbound | ||||||
1ibsA02 | Analogue:_CD | Unbound | Unbound | Unbound | Analogue:ABM | Unbound | Unbound | ||||||
1ibsB02 | 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 | LYS 197 | |||||||||
1dkrB01 | LYS 197 | |||||||||
1dkuA01 | LYS 197 | |||||||||
1dkuB01 | LYS 197 | |||||||||
1ibsA01 | LYS 197 | |||||||||
1ibsB01 | LYS 197 | |||||||||
1dkrA02 | ARG 101 | ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding) | ||||||||
1dkrB02 | ARG 101 | ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding) | ||||||||
1dkuA02 | ARG 101 | ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding) | ||||||||
1dkuB02 | ARG 101 | ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding) | ||||||||
1ibsA02 | ARG 101 | ASP 133;HIS 135;ASP 144;ASP 148(magnesium binding) | ||||||||
1ibsB02 | 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. |
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. |
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, |
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 |
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Created | Updated |
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2004-03-18 | 2009-02-26 |