P09559 (KPPR_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phosphoribulokinase, chloroplastic Short name=PRK Short name=PRKase EC=2.7.1.19 Alternative name(s): Phosphopentokinase
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast.
Sequence similarities	Belongs to the phosphoribulokinase family.
Sequence caution	The sequence AAA34036.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Calvin cycle Photosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribulokinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 51	51	Chloroplast Ref.3 Ref.4
	Chain	52 – 402	351	Phosphoribulokinase, chloroplastic		PRO_0000025754
Amino acid modifications
	Disulfide bond	67 ↔ 106		Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P09559 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 450759B96A675C6B	FASTA	402	45,007
	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

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.
PIR	S02099.
3D structure databases
ProteinModelPortal	P09559.
ModBase	Search...
Proteomic databases
PRIDE	P09559.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00116.
Family and domain databases
InterPro	IPR006082. PRK. IPR006083. PRK/URK. [Graphical view]
Pfam	PF00485. PRK. 1 hit. [Graphical view]
PRINTS	PR00478. PHRIBLKINASE.
PROSITE	PS00567. PHOSPHORIBULOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPPR_SPIOL

Accession

Primary (citable) accession number: P09559

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program