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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of ribose 1,5-bisphosphate. Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.UniRule annotation

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase (prs), Ribose-phosphate pyrophosphokinase (prs)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101Ribose-5-phosphateUniRule annotation
Metal bindingi134 – 1341MagnesiumUniRule annotation
Metal bindingi136 – 1361MagnesiumUniRule annotation
Binding sitei136 – 1361ATPUniRule annotation
Binding sitei141 – 1411ATPUniRule annotation
Metal bindingi145 – 1451MagnesiumUniRule annotation
Metal bindingi149 – 1491MagnesiumUniRule annotation
Binding sitei175 – 1751Ribose-5-phosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 453ATPUniRule annotation
Nucleotide bindingi102 – 1054ATPUniRule annotation
Nucleotide bindingi149 – 1502ATPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB-HAMAP
  • ribose phosphate diphosphokinase activity Source: TIGR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciANTHRA:PRS-MONOMER.
BANT260799:GJAJ-56-MONOMER.
BANT261594:GJ7F-58-MONOMER.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinaseUniRule annotation (EC:2.7.6.1UniRule annotation)
Short name:
RPPKUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthaseUniRule annotation
Phosphoribosyl pyrophosphate synthaseUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthaseUniRule annotation
Short name:
PRPPaseUniRule annotation
Gene namesi
Name:prsUniRule annotation
Ordered Locus Names:BA_0049, GBAA_0049, BAS0049
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Ribose-phosphate pyrophosphokinasePRO_0000141106Add
BLAST

Proteomic databases

PRIDEiQ81VZ0.

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_0049.

Structurei

3D structure databases

ProteinModelPortaliQ81VZ0.
SMRiQ81VZ0. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2003Ribose-5-phosphate bindingUniRule annotation
Regioni225 – 2328Ribose-5-phosphate bindingUniRule annotation
Regioni311 – 3133Ribose-5-phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210451.
KOiK00948.
OMAiDGEIMVE.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81VZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTQYLNSNL KVFSLNSNKE LAEQIAKHIG VGLGKCSVDR FSDGEVQINI
60 70 80 90 100
EESIRGCDVF IIQSTSFPVN EHIMELLIMI DALKRASAKT INIVIPYYGY
110 120 130 140 150
ARQDRKARSR EPITSKLVAN LLETAGATRV ITLDLHAPQI QGFFDIPIDH
160 170 180 190 200
LMGVPILSDY FETKGLKDIV IVSPDHGGVT RARKMADRLK APIAIIDKRR
210 220 230 240 250
PRPNVSEVMN IIGNIEGKTA ILIDDIIDTA GTITLAANAL VENGASEVYA
260 270 280 290 300
CCTHPVLSGP AIERIQNSNI KELVVTNSIV LPEEKKIDKV HELSVAPLIG
310
EAIIRVYEEE SVSVLFN
Length:317
Mass (Da):34,836
Last modified:June 1, 2003 - v1
Checksum:i16414CD5645DA23A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP24104.1.
AE017334 Genomic DNA. Translation: AAT29127.1.
AE017225 Genomic DNA. Translation: AAT52387.1.
RefSeqiNP_842618.1. NC_003997.3.
WP_000107420.1. NZ_LHUO01000018.1.
YP_026336.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP24104; AAP24104; BA_0049.
AAT29127; AAT29127; GBAA_0049.
AAT52387; AAT52387; BAS0049.
GeneIDi1084386.
23122061.
2851335.
KEGGiban:BA_0049.
bar:GBAA_0049.
bat:BAS0049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP24104.1.
AE017334 Genomic DNA. Translation: AAT29127.1.
AE017225 Genomic DNA. Translation: AAT52387.1.
RefSeqiNP_842618.1. NC_003997.3.
WP_000107420.1. NZ_LHUO01000018.1.
YP_026336.1. NC_005945.1.

3D structure databases

ProteinModelPortaliQ81VZ0.
SMRiQ81VZ0. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_0049.

Proteomic databases

PRIDEiQ81VZ0.

Protocols and materials databases

DNASUi1084386.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP24104; AAP24104; BA_0049.
AAT29127; AAT29127; GBAA_0049.
AAT52387; AAT52387; BAS0049.
GeneIDi1084386.
23122061.
2851335.
KEGGiban:BA_0049.
bar:GBAA_0049.
bat:BAS0049.

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210451.
KOiK00948.
OMAiDGEIMVE.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciANTHRA:PRS-MONOMER.
BANT260799:GJAJ-56-MONOMER.
BANT261594:GJ7F-58-MONOMER.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPRS_BACAN
AccessioniPrimary (citable) accession number: Q81VZ0
Secondary accession number(s): Q6I4Z4, Q6KYN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: September 7, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.