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ECOLI:KPRS

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) No Information Provided. (synonyms: prsA)
Protein Name(s) Ribose-phosphate pyrophosphokinase (ECO:0000255 with HAMAP-Rule:MF_00583, ECO:0000303 with PMID:2542328[1], ECO:0000303 with PMID:3009477[2], ECO:0000303 with PMID:6290219[3])

RPPK (ECO:0000255 with HAMAP-Rule:MF_00583, ECO:0000303 with PMID:2542328[1], ECO:0000303 with PMID:3009477[2], ECO:0000303 with PMID:6290219[3]) 5-phospho-D-ribosyl alpha-1-diphosphate (ECO:0000255 with HAMAP-Rule:MF_00583) Phosphoribosyl diphosphate synthase (ECO:0000255 with HAMAP-Rule:MF_00583) Phosphoribosyl pyrophosphate synthase (ECO:0000255 with HAMAP-Rule:MF_00583, ECO:0000303 with PMID:2542328[1], ECO:0000303 with PMID:3009477[2], ECO:0000303 with PMID:6290219[3]) P-Rib-PP synthase (ECO:0000255 with HAMAP-Rule:MF_00583) PRPP synthase (ECO:0000255 with HAMAP-Rule:MF_00583) PRPPase (ECO:0000255 with HAMAP-Rule:MF_00583)

External Links
UniProt P0A717
EMBL M13174
U00096
AP009048
PIR D64867
RefSeq NP_415725.1
YP_489474.1
ProteinModelPortal P0A717
SMR P0A717
DIP DIP-35839N
IntAct P0A717
MINT MINT-1221689
STRING 511145.b1207
PaxDb P0A717
PRIDE P0A717
EnsemblBacteria AAC74291
BAA36065
GeneID 12931819
945772
KEGG ecj:Y75_p1179
eco:b1207
PATRIC 32117666
EchoBASE EB0767
EcoGene EG10774
eggNOG COG0462
HOGENOM HOG000210452
InParanoid P0A717
KO K00948
OMA QMANEIK
OrthoDB EOG6Z99XQ
PhylomeDB P0A717
BioCyc EcoCyc:PRPPSYN-MONOMER
ECOL316407:JW1198-MONOMER
MetaCyc:PRPPSYN-MONOMER
UniPathway UPA00087
PRO PR:P0A717
Proteomes UP000000318
UP000000625
Genevestigator P0A717
GO GO:0005737
GO:0005524
GO:0016301
GO:0000287
GO:0042301
GO:0004749
GO:0006015
GO:0009165
GO:0009156
Gene3D 3.40.50.2020
HAMAP MF_00583_B
InterPro IPR000842
IPR029099
IPR029057
IPR005946
Pfam PF14572
PF13793
SUPFAM SSF53271
TIGRFAMs TIGR01251
PROSITE PS00114

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0009165

nucleotide biosynthetic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000025022
RGD:3415
RGD:61955

P

Seeded From UniProt

complete

involved_in

GO:0006164

purine nucleotide biosynthetic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000025022
UniProtKB:P60891

P

Seeded From UniProt

complete

involved_in

GO:0006015

5-phosphoribose 1-diphosphate biosynthetic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10774
PANTHER:PTN000025022
RGD:3415
RGD:61955
SGD:S000000164
SGD:S000000901
SGD:S000001003
SGD:S000001664
SGD:S000005422
UniProtKB:P9WKE3

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000025022
SGD:S000001664
TAIR:locus:2045590

C

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10774
PANTHER:PTN000025022
RGD:3415
RGD:61955
UniProtKB:P60891
UniProtKB:P9WKE3

F

Seeded From UniProt

complete

part_of

GO:0002189

ribose phosphate diphosphokinase complex

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000025022
RGD:3415
RGD:61955
RGD:620206
RGD:620207
SGD:S000000164
SGD:S000000901
SGD:S000001003
SGD:S000001664
SGD:S000005422

C

Seeded From UniProt

complete

enables

GO:0042301

phosphate ion binding

PMID:10954724[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006015

5-phosphoribose 1-diphosphate biosynthetic process

PMID:6290219[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

PMID:3009477[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:9125530[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000842
InterPro:IPR005946

F

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000842
InterPro:IPR005946
InterPro:IPR037515

F

Seeded From UniProt

complete

involved_in

GO:0009116

nucleoside metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000836

P

Seeded From UniProt

complete

involved_in

GO:0009156

ribonucleoside monophosphate biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000842

P

Seeded From UniProt

complete

involved_in

GO:0009165

nucleotide biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005946

P

Seeded From UniProt

complete

involved_in

GO:0044249

cellular biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000842

P

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.6.1

F

Seeded From UniProt

complete

involved_in

GO:0009156

ribonucleoside monophosphate biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101710

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101710

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101710

C

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101710

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0009165

nucleotide biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0545

P

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

involved_in

GO:0006015

5-phosphoribose 1-diphosphate biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00087

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Bower, SG et al. (1989) Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J. Biol. Chem. 264 10287-91 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Hove-Jensen, B et al. (1986) Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene. J. Biol. Chem. 261 6765-71 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Hove-Jensen, B & Nygaard, P (1982) Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification of a mutant enzyme. Eur. J. Biochem. 126 327-32 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. ↑ Willemoës, M et al. (2000) Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase. J. Biol. Chem. 275 35408-12 PubMed GONUTS page
  6. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  8. ↑ Willemoës, M & Hove-Jensen, B (1997) Binding of divalent magnesium by Escherichia coli phosphoribosyl diphosphate synthetase. Biochemistry 36 5078-83 PubMed GONUTS page
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