Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25697 (KPPR_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribulokinase, chloroplastic

Short name=PRK
Short name=PRKase
EC=2.7.1.19
Alternative name(s):
Phosphopentokinase
Gene names
Ordered Locus Names:At1g32060
ORF Names:T12O21.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate.

Enzyme regulation

Light regulated via thioredoxin by reversible oxidation/reduction of sulfhydryl/disulfide groups.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the phosphoribulokinase family.

Ontologies

Keywords
   Biological processCalvin cycle
Photosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from expression pattern PubMed 17028151. Source: TAIR

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to cold

Inferred from expression pattern PubMed 16923014. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay PubMed 12938931. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay PubMed 15322131. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

stromule

Inferred from direct assay PubMed 16923014. Source: TAIR

thylakoid

Inferred from direct assay PubMed 16648217. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribulokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 16258009. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRX3Q424031EBI-449190,EBI-449157

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Chloroplast
Chain47 – 395349Phosphoribulokinase, chloroplastic
PRO_0000025751

Amino acid modifications

Disulfide bond61 ↔ 100 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25697 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 4660A92EF7E39BC6

FASTA39544,464
        10         20         30         40         50         60 
MAVSTIYSTQ ALNSTHFLTS SSSSKQVFLY RRQPQTNRRF NTLITCAQET IVIGLAADSG 

        70         80         90        100        110        120 
CGKSTFMRRL TSVFGGAAKP PKGGNPDSNT LISDTTTVIC LDDYHSLDRY GRKEQKVTAL 

       130        140        150        160        170        180 
DPRANDFDLM YEQVKALKNG IAVEKPIYNH VTGLLDPPEL IQPPKILVIE GLHPMFDERV 

       190        200        210        220        230        240 
RDLLDFSIYL DISNEVKFAW KIQRDMAERG HSLESIKASI EARKPDFDAF IDPQKQYADA 

       250        260        270        280        290        300 
VIEVLPTTLI PDDNEGKVLR VRLIMKEGVK YFSPVYLFDE GSTISWIPCG RKLTCSYPGI 

       310        320        330        340        350        360 
KFNYEPDSYF DHEVSVLEMD GQFDRLDELI YVESHLSNLS TKFYGEVTQQ MLKHADFPGS 

       370        380        390 
NNGTGLFQTI VGLKIRDLYE QLIANKATAR AEAKA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a cDNA clone encoding chloroplast phosphoribulokinase from Arabidopsis thaliana."
Horsnell P.R., Raines C.A.
Plant Mol. Biol. 17:183-184(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. C24.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58149 mRNA. Translation: CAA41155.1.
AC074309 Genomic DNA. Translation: AAG50797.1.
CP002684 Genomic DNA. Translation: AEE31430.1.
AY044335 mRNA. Translation: AAK73276.1.
AY128355 mRNA. Translation: AAM91558.1.
BT000019 mRNA. Translation: AAN15338.1.
AY084576 mRNA. Translation: AAM61142.1.
PIRS16583.
RefSeqNP_174486.1. NM_102940.5.
UniGeneAt.22659.

3D structure databases

ProteinModelPortalP25697.
SMRP25697. Positions 47-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid25332. 3 interactions.
IntActP25697. 2 interactions.
STRING3702.AT1G32060.1-P.

2D gel databases

SWISS-2DPAGEP25697.
World-2DPAGE0003:P25697.

Proteomic databases

PaxDbP25697.
PRIDEP25697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G32060.1; AT1G32060.1; AT1G32060.
GeneID840098.
KEGGath:AT1G32060.

Organism-specific databases

TAIRAT1G32060.

Phylogenomic databases

eggNOGCOG0572.
HOGENOMHOG000230117.
InParanoidP25697.
KOK00855.
OMAMKPIYNH.
PhylomeDBP25697.

Enzyme and pathway databases

BioCycARA:AT1G32060-MONOMER.
MetaCyc:AT1G32060-MONOMER.
UniPathwayUPA00116.

Gene expression databases

GenevestigatorP25697.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR006082. PRK.
IPR006083. PRK/URK.
[Graphical view]
PfamPF00485. PRK. 1 hit.
[Graphical view]
PRINTSPR00478. PHRIBLKINASE.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00567. PHOSPHORIBULOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPPR_ARATH
AccessionPrimary (citable) accession number: P25697
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 11, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names