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P42816 (KPRS_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase

Short name=RPPK
EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase
Short name=P-Rib-PP synthase
Short name=PRPP synthase
Gene names
Name:prs
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00583_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00583_B

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. HAMAP MF_00583_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00583_B.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Ribose-phosphate pyrophosphokinase HAMAP MF_00583_B
PRO_0000141107

Regions

Region215 – 22814Binding of phosphoribosylpyrophosphate Potential

Sites

Metal binding1321Magnesium Potential
Metal binding1341Magnesium Potential
Metal binding1431Magnesium Potential
Metal binding1471Magnesium Potential

Sequences

Sequence LengthMass (Da)Tools
P42816 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CD661ABA511DEAED

FASTA31534,533
        10         20         30         40         50         60 
MSDCQHQLKL FALNSNMKLA KEIAEVMGIE LGKCSVSRFS DGEIQINIEE SIRGDDVFVI 

        70         80         90        100        110        120 
QSTSVPVNEH LMELLIMIDA LKRASARTIN IVMPYYGYAR QDRKARSRNP ITAKLVANLL 

       130        140        150        160        170        180 
ETAGASRVIT LDLHAPQIQG FFDIPIDHLM GVPILADYFK SKQLEDIVVV SPDHGGVTRA 

       190        200        210        220        230        240 
RKLADRLKAP IAIIDKRRPK PNVAEVMNIV GQVAGKTAIL IDDIIDTAGT ITLAANALAE 

       250        260        270        280        290        300 
SGAKEVYACC THPVLSGPAI ERIQSSKIKE LVVTNSIALP EEKKIDKIVK LSVRPLIAEA 

       310 
ITRVYEMKSV SVLFD 

« Hide

References

[1]"Bacillus caldolyticus prs gene encoding phosphoribosyl-diphosphate synthase."
Krath B.N., Hove-Jensen B.
Gene 176:73-79(1996) [PubMed: 8918235] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 405 / NBRC 15313 / YP-T.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83708 Genomic DNA. Translation: CAA58682.1.
PIRJC5093.

3D structure databases

ProteinModelPortalP42816.
SMRP42816. Positions 8-314.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00583_B. RibP_PPkinase_B.
[Tree]
InterProIPR000842. PRib_PP_synth_CS.
IPR000836. PRibTrfase.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. RibP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPRS_BACCL
AccessionPrimary (citable) accession number: P42816
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 31, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families