Plastidial pyruvate kinase 2 precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q9FLW9 (PKP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Plastidial pyruvate kinase 2
Short name=PKp2
EC=2.7.1.40

Alternative name(s):
Plastidial pyruvate kinase 1
Short name=PKP1
Pyruvate kinase III
Pyruvate kinase isozyme B1, chloroplastic
Short name=PKP-BETA1
Short name=Plastidic pyruvate kinase beta subunit 1

Gene names

Name:	PKP2
Synonyms:	PKP1
Ordered Locus Names:	At5g52920
ORF Names:	MXC20.15

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	579 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)

Function	Required for plastidial pyruvate kinase activity. Involved in seed oil accumulation, embryo development and seed storage compounds mobilization upon germination. Ref.9 Ref.10 Ref.11
Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Ref.9 Potassium. Ref.9
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Oligomer of alpha and beta subunits. Ref.9
Subcellular location	Plastid › chloroplast stroma. Mitochondrion Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14.
Tissue specificity	Mostly expressed in seeds, and, to a lower extent, in roots, leaves (veins and trichomes), inflorescences, siliques, pollen (grains and tubes) and flowers (sepals and petals). Ref.9 Ref.10
Developmental stage	In seeds, accumulates in endosperm and embryo. In torpedo-shaped embryos, restricted to the hypocotyl and in the outer parts of the young cotyledons. In later embryo stages, present in all tissues except root tips. Ref.10
Induction	Repressed by cadmium.
Disruption phenotype	Reduced plastidial pyruvate kinase activity and altered seed oil content leading to wrinkled seeds, retarded embryo elongation and reduced seed germination. Ref.9 Ref.10
Sequence similarities	Belongs to the pyruvate kinase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.8-8.0. Ref.9 Ref.10

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from mutant phenotype Ref.10. Source: TAIR glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway response to cadmium ion Inferred from expression pattern Ref.8. Source: TAIR seed maturation Inferred from mutant phenotype Ref.9 Ref.10. Source: UniProtKB
Cellular_component	chloroplast stroma Inferred from direct assay Ref.7 Ref.9 Ref.13. Source: TAIR mitochondrion Inferred from direct assay Ref.6. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from direct assay Ref.9. Source: UniProtKB potassium ion binding Inferred from direct assay Ref.9. Source: UniProtKB pyruvate kinase activity Inferred from direct assay Ref.9. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 63

Chloroplast Potential

Chain

64 – 579

516

Plastidial pyruvate kinase 2

PRO_0000416988

Sites

Metal binding

142

Potassium By similarity

Metal binding

175

Potassium By similarity

Metal binding

176

Potassium; via carbonyl oxygen By similarity

Metal binding

327

Magnesium Potential

Metal binding

351

Magnesium By similarity

Binding site

140

Substrate By similarity

Binding site

350

Substrate; via amide nitrogen By similarity

Binding site

351

Substrate; via amide nitrogen By similarity

Binding site

383

Substrate By similarity

Site

325

Transition state stabilizer By similarity

Experimental info

Sequence conflict

342

S → P in AAK82461. Ref.3

Sequence conflict

342

S → P in AAM10281. Ref.3

Sequence conflict

383

T → A in BAD93771. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FLW9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9A728605C826B4D3
Show »

FASTA

579

63,522

        10         20         30         40         50         60 
MAQVVATRSI QGSMLSPNGG SVSTRSEKLL KPASFAVKVL GNEAKRSGRV SVRSRRVVDT 

        70         80         90        100        110        120 
TVRSARVETE VIPVSPEDVP NREEQLERLL EMQQFGDTSV GMWSKPTVRR KTKIVCTVGP 

       130        140        150        160        170        180 
STNTREMIWK LAEAGMNVAR MNMSHGDHAS HKKVIDLVKE YNAQTKDNTI AIMLDTKGPE 

       190        200        210        220        230        240 
VRSGDLPQPI MLDPGQEFTF TIERGVSTPS CVSVNYDDFV NDVEAGDMLL VDGGMMSFMV 

       250        260        270        280        290        300 
KSKTKDSVKC EVVDGGELKS RRHLNVRGKS ATLPSITEKD WEDIKFGVEN KVDFYAVSFV 

       310        320        330        340        350        360 
KDAQVVHELK KYLQNSGADI HVIVKIESAD SIPNLHSIIT ASDGAMVARG DLGAELPIEE 

       370        380        390        400        410        420 
VPILQEEIIN LCRSMGKAVI VATNMLESMI VHPTPTRAEV SDIAIAVREG ADAVMLSGET 

       430        440        450        460        470        480 
AHGKFPLKAA GVMHTVALRT EATITSGEMP PNLGQAFKNH MSEMFAYHAT MMSNTLGTST 

       490        500        510        520        530        540 
VVFTRTGFMA ILLSHYRPSG TIYAFTNEKK IQQRLALYQG VCPIYMEFTD DAEETFANAL 

       550        560        570 
ATLLKQGMVK KGEEIAIVQS GTQPIWRSQS THNIQVRKV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones." Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases 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].
[6]	"Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells." Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R., Leaver C.J., Sweetlove L.J. Plant Cell 15:2140-2151(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts." Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J. Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses." Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V., Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C., Ezan E., Garin J., Bourguignon J. Proteomics 6:2180-2198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY CADMIUM [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: cv. Columbia.
[9]	"A heteromeric plastidic pyruvate kinase complex involved in seed oil biosynthesis in Arabidopsis." Andre C., Froehlich J.E., Moll M.R., Benning C. Plant Cell 19:2006-2022(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY.
[10]	"Function of plastidial pyruvate kinases in seeds of Arabidopsis thaliana." Baud S., Wuilleme S., Dubreucq B., de Almeida A., Vuagnat C., Lepiniec L., Miquel M., Rochat C. Plant J. 52:405-419(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia and cv. Wassilewskija.
[11]	"Arabidopsis seedlings deficient in a plastidic pyruvate kinase are unable to utilize seed storage compounds for germination and establishment." Andre C., Benning C. Plant Physiol. 145:1670-1680(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins." Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N. Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering." Olinares P.D., Ponnala L., van Wijk K.J. Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB009055 Genomic DNA. Translation: BAB10440.1. CP002688 Genomic DNA. Translation: AED96278.1. AY048198 mRNA. Translation: AAK82461.1. AY091682 mRNA. Translation: AAM10281.1. AK220807 mRNA. Translation: BAD94078.1. AK220873 mRNA. Translation: BAD94256.1. AK221740 mRNA. Translation: BAD93771.1. AY084507 mRNA. Translation: AAM61075.1.
IPI	IPI00536297.
RefSeq	NP_200104.1. NM_124670.2.
UniGene	At.20836.
3D structure databases
ProteinModelPortal	Q9FLW9.
SMR	Q9FLW9. Positions 110-564.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G52920.1-P.
Proteomic databases
PRIDE	Q9FLW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G52920.1; AT5G52920.1; AT5G52920.
GeneID	835369.
KEGG	ath:AT5G52920.
Organism-specific databases
TAIR	At5g52920.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
InParanoid	Q9FLW9.
KO	K00873.
OMA	ERCDESI.
PhylomeDB	Q9FLW9.
ProtClustDB	PLN02623.
Enzyme and pathway databases
SABIO-RK	Q9FLW9.
UniPathway	UPA00109; UER00188.
Gene expression databases
ArrayExpress	Q9FLW9.
Genevestigator	Q9FLW9.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PKP2_ARATH

Accession

Primary (citable) accession number: Q9FLW9
Secondary accession number(s): Q56XD5

Q94AG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	March 1, 2001
Last modified:	May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents