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P46585 (KPR1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 1
EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 1
Gene names
Name:PRS1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length321 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.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Ribose-phosphate pyrophosphokinase 1
PRO_0000141085

Sites

Metal binding1311Magnesium Potential
Metal binding1331Magnesium Potential
Metal binding1421Magnesium Potential
Metal binding1461Magnesium Potential

Sequences

Sequence LengthMass (Da)Tools
P46585 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: AC70534163AA5BEB

FASTA32135,278
        10         20         30         40         50         60 
MSTNSIKLLA SDVHRGLAEL VSKRLGLRLT PSELKRESTG EVQFSIGESV RDEDIFIICQ 

        70         80         90        100        110        120 
IGSGEVNDRV FELMIMINAC KTASARRITV ILPNFPYARQ DRKDKSRAPI TAKLMADMLT 

       130        140        150        160        170        180 
TAGCDHVITM DLHASQIQGF FDVPVDNLYA EPSVVRYIKE TIDYSEAIII SSDAGGAKRA 

       190        200        210        220        230        240 
AGLADRLDLN FELIHKERAR ANEVSRMVLV VDVTDKICVI VDDMADTCGT LAKAAEVLLD 

       250        260        270        280        290        300 
NNAKDVIAIV THGILSGNAI KNINNSKLKK VVCTNTVPFE DKLKLCLKLD TIDISAVIAE 

       310        320 
SIRRLHNGES ISYLFKNAPC K

« Hide

References

[1]"Isolation of phosphoribosylpyrophosphate synthetase (PRS1) gene from Candida albicans."
Payne T.L., Calderone R.A.
Yeast 11:1295-1302(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 4918.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U23934 Genomic DNA. Translation: AAA97558.1.
PIRS60393.

3D structure databases

ProteinModelPortalP46585.
SMRP46585. Positions 6-315.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0462.

Family and domain databases

InterProIPR000842. PRib_PP_synth_CS.
IPR000836. PRibTrfase_dom.
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 nameKPR1_CANAX
AccessionPrimary (citable) accession number: P46585
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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