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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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)
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 sitei112 – 1121Ribose-5-phosphateUniRule annotation
Metal bindingi136 – 1361MagnesiumUniRule annotation
Metal bindingi138 – 1381MagnesiumUniRule annotation
Binding sitei138 – 1381ATPUniRule annotation
Binding sitei143 – 1431ATPUniRule annotation
Metal bindingi147 – 1471MagnesiumUniRule annotation
Metal bindingi151 – 1511MagnesiumUniRule annotation
Binding sitei178 – 1781Ribose-5-phosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 473ATPUniRule annotation
Nucleotide bindingi104 – 1074ATPUniRule annotation
Nucleotide bindingi151 – 1522ATPUniRule annotation

GO - Molecular functioni

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

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:SCO3123
ORF Names:SCE66.02
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 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 – 324324Ribose-phosphate pyrophosphokinasePRO_0000141201Add
BLAST

Proteomic databases

PRIDEiQ9K3U0.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO3123.

Structurei

3D structure databases

ProteinModelPortaliQ9K3U0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2033Ribose-5-phosphate bindingUniRule annotation
Regioni230 – 2378Ribose-5-phosphate bindingUniRule annotation
Regioni316 – 3183Ribose-5-phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ribose-phosphate pyrophosphokinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210449.
InParanoidiQ9K3U0.
KOiK00948.
OMAiDGEIMVE.
OrthoDBiEOG6Z99XQ.
PhylomeDBiQ9K3U0.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
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.

Q9K3U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGIKTTGEK KMMFFSGRAH PELAEEVAQQ LGVGVVPTKA FDFANGEIYV
60 70 80 90 100
RYQESARGAD CFLIQSHTAP INKWVMEQLI MIDALKRASA RSITVIVPFY
110 120 130 140 150
GYARQDKKHR GREPISARLI ADLMKTAGAD RILAVDLHTD QIQGFFDGPV
160 170 180 190 200
DHLFALPLLA DYVGAKVDRS KLTVVSPDAG RVRVADRWCD RLGAPLAIVH
210 220 230 240 250
KRRDKDVANQ VTVHEVVGDV KGRICVLVDD MIDTGGTICA AADALFAHGA
260 270 280 290 300
EDVIVTATHG VLSGPAADRL KNSKVSEFVF TNTLPSASEL ELDKITVLSI
310 320
APTIARAVRE VFEDGSVTSL FDEQ
Length:324
Mass (Da):35,271
Last modified:October 1, 2000 - v1
Checksum:i91C7FA6549AC1641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939115 Genomic DNA. Translation: CAB95916.1.
RefSeqiNP_627340.1. NC_003888.3.
WP_003975691.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB95916; CAB95916; CAB95916.
GeneIDi1098557.
KEGGisco:SCO3123.
PATRICi23735994. VBIStrCoe124346_3187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939115 Genomic DNA. Translation: CAB95916.1.
RefSeqiNP_627340.1. NC_003888.3.
WP_003975691.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9K3U0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO3123.

Proteomic databases

PRIDEiQ9K3U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB95916; CAB95916; CAB95916.
GeneIDi1098557.
KEGGisco:SCO3123.
PATRICi23735994. VBIStrCoe124346_3187.

Phylogenomic databases

eggNOGiENOG4105C5T. Bacteria.
COG0462. LUCA.
HOGENOMiHOG000210449.
InParanoidiQ9K3U0.
KOiK00948.
OMAiDGEIMVE.
OrthoDBiEOG6Z99XQ.
PhylomeDBiQ9K3U0.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiKPRS_STRCO
AccessioniPrimary (citable) accession number: Q9K3U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 1, 2000
Last modified: November 11, 2015
This is version 93 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.