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MYCTU:KPRS

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) prs (ECO:0000255 with HAMAP-Rule:MF_00583) (synonyms: prsA)
Protein Name(s) Ribose-phosphate pyrophosphokinase (ECO:0000255 with HAMAP-Rule:MF_00583)

RPPK (ECO:0000255 with HAMAP-Rule:MF_00583) 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) 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 P9WKE3
EMBL AL123456
PIR D70622
RefSeq NP_215533.1
WP_003405263.1
ProteinModelPortal P9WKE3
SMR P9WKE3
STRING 83332.Rv1017c
PaxDb P9WKE3
EnsemblBacteria CCP43767
GeneID 885993
KEGG mtu:Rv1017c
TubercuList Rv1017c
eggNOG ENOG4105C5T
COG0462
KO K00948
OMA DGEIMVE
PhylomeDB P9WKE3
UniPathway UPA00087
Proteomes UP000001584
GO GO:0005618
GO:0005737
GO:0005886
GO:0005524
GO:0016301
GO:0000287
GO:0030145
GO:0004749
GO:0006015
GO:0040007
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

part_of

GO:0005886

plasma membrane

PMID:15525680[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:14532352[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:20825248[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:21045009[4]

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:21085589[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006015

5-phosphoribose 1-diphosphate biosynthetic process

PMID:21045009[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

PMID:21085589[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004749

ribose phosphate diphosphokinase activity

PMID:21045009[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:21045009[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009165

nucleotide biosynthetic process

PMID:21873635[6]

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[6]

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[6]

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[6]

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[6]

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[6]

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: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

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

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

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

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

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

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

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

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

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

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

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: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:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

involved_in

GO:0045227

capsule polysaccharide biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00963

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. ↑ Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
  2. ↑ Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
  3. ↑ Wolfe, LM et al. (2010) Proteomic definition of the cell wall of Mycobacterium tuberculosis. J. Proteome Res. 9 5816-26 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 Alderwick, LJ et al. (2011) Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase. Glycobiology 21 410-25 PubMed GONUTS page
  5. ↑ 5.0 5.1 Lucarelli, AP et al. (2010) Mycobacterium tuberculosis phosphoribosylpyrophosphate synthetase: biochemical features of a crucial enzyme for mycobacterial cell wall biosynthesis. PLoS ONE 5 e15494 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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