Reviewed, UniProtKB/Swiss-Prot P25697 (KPPR_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphoribulokinase, chloroplastic
      Short name=PRKase
      Short name=PRK
    EC=2.7.1.19
Alternative name(s):
    Phosphopentokinase

Gene names

Ordered Locus Names:	At1g32060
ORF Names:	T12O21.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	395 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.

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	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from expression pattern. Source: TAIR reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW response to cold Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribulokinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449190,EBI-449157

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Chloroplast
	Chain	47 – 395	349	Phosphoribulokinase, chloroplastic		PRO_0000025751
Amino acid modifications
	Disulfide bond	61 ↔ 100		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25697-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 4660A92EF7E39BC6	FASTA	395	44,464
	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

References

	« Hide 'large scale' referencesShow '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: 1651130] [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. , 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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58149 mRNA. Translation: CAA41155.1. AC074309 Genomic DNA. Translation: AAG50797.1. AY044335 mRNA. Translation: AAK73276.1. AY128355 mRNA. Translation: AAM91558.1. BT000019 mRNA. Translation: AAN15338.1. AY084576 mRNA. Translation: AAM61142.1.
IPI	IPI00516350.
PIR	S16583.
RefSeq	NP_174486.1.
UniGene	At.22659
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P25697. 2 interactions.
2-D gel databases
SWISS-2DPAGE	P25697.
Proteomic databases
PRIDE	P25697.
ProMEX	P25697.
Genome annotation databases
GeneID	840098.
GenomeReviews	Gene locus AT1G32060 in contig CT485782_GR.
KEGG	ath:AT1G32060.
NMPDR	fig|3702.1.peg.3554.
Organism-specific databases
TAIR	At1g32060.
Phylogenomic databases
OMA	P25697. RLIMKEG.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G32060-MON.
BRENDA	2.7.1.19. 302.
Gene expression databases
ArrayExpress	P25697.
GermOnline	AT1G32060. Arabidopsis thaliana.
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_ARATH

Accession

Primary (citable) accession number: P25697

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)