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P09559 (KPPR_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:
Phosphoribulokinase, chloroplastic

Short name=PRK
Short name=PRKase
EC=2.7.1.19
Alternative name(s):
Phosphopentokinase
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length402 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.

Sequence caution

The sequence AAA34036.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCalvin cycle
Photosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processreductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribulokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5151Chloroplast Ref.3 Ref.4
Chain52 – 402351Phosphoribulokinase, chloroplastic
PRO_0000025754

Amino acid modifications

Disulfide bond67 ↔ 106 Ref.5

Sequences

Sequence LengthMass (Da)Tools
P09559 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 450759B96A675C6B

FASTA40245,007
        10         20         30         40         50         60 
MAVCTVYTIP TTTHLGSSFN QNNKQVFFNY KRSSSSNNTL FTTRPSYVIT CSQQQTIVIG 

        70         80         90        100        110        120 
LAADSGCGKS TFMRRLTSVF GGAAEPPKGG NPDSNTLISD TTTVICLDDF HSLDRNGRKV 

       130        140        150        160        170        180 
EKVTALDPKA NDFDLMYEQV KALKEGKAVD KPIYNHVSGL LDPPELIQPP KILVIEGLHP 

       190        200        210        220        230        240 
MYDARVRELL DFSIYLDISN EVKFAWKIQR DMKERGHSLE SIKASIESRK PDFDAYIDPQ 

       250        260        270        280        290        300 
KQHADVVIEV LPTELIPDDD EGKVLRVRMI QKEGVKFFNP VYLFDEGSTI SWIPCGRKLT 

       310        320        330        340        350        360 
CSYPGIKFSY GPDTFYGNEV TVVEMDGMFD RLDELIYVES HLSNLSTKFY GEVTQQMLKH 

       370        380        390        400 
QNFPGSNNGT GFFQTIIGLK IRDLFEQLVA SRSTATATAA KA 

« Hide

References

[1]"Nucleotide sequence of spinach cDNA encoding phosphoribulokinase."
Roesler K.R., Ogren W.L.
Nucleic Acids Res. 16:7192-7192(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and sequencing of cDNA encoding the mature form of phosphoribulokinase from spinach."
Milanez S., Mural R.J.
Gene 66:55-63(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-402.
[3]"Purification and characterization of ribulose-5-phosphate kinase from spinach."
Porter M.A., Milanez S., Stringer C.D., Hartman F.C.
Arch. Biochem. Biophys. 245:14-23(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-69.
[4]"Commonality of catalytic and regulatory sites of spinach phosphoribulokinase: characterization of a tryptic peptide that contains an essential cysteinyl residue."
Porter M.A., Hartman F.C.
Biochemistry 25:7314-7318(1986)
Cited for: PROTEIN SEQUENCE OF 52-69.
[5]"Characterization of the regulatory thioredoxin site of phosphoribulokinase."
Porter M.A., Stringer C.D., Hartman F.C.
J. Biol. Chem. 263:123-129(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND, PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07654 mRNA. Translation: CAA30499.1.
M21338 mRNA. Translation: AAA34036.1. Different initiation.
PIRS02099.

3D structure databases

ProteinModelPortalP09559.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP09559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00116.

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_SPIOL
AccessionPrimary (citable) accession number: P09559
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 76 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