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Q93Z53 (PKP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plastidial pyruvate kinase 3, chloroplastic

Short name=PKp3
EC=2.7.1.40
Alternative name(s):
Pyruvate kinase I
Pyruvate kinase isozyme B2, chloroplastic
Short name=PKP-BETA2
Short name=Plastidic pyruvate kinase beta subunit 2
Gene names
Name:PKP3
Ordered Locus Names:At1g32440
ORF Names:F5D14.22
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for plastidial pyruvate kinase activity By similarity.

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium. Ref.4

Potassium. Ref.4

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Oligomer of alpha and beta subunits. Ref.4

Subcellular location

Plastidchloroplast stroma Ref.4 Ref.6.

Tissue specificity

Expressed at low levels in roots, leaves, inflorescences, siliques, pollen, seeds and flowers. Ref.4 Ref.5

Sequence similarities

Belongs to the pyruvate kinase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.8-8.0. Ref.4

Sequence caution

The sequence AAF81342.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast Potential
Chain56 – 571516Plastidial pyruvate kinase 3, chloroplastic
PRO_0000416989

Sites

Metal binding1311Potassium By similarity
Metal binding1641Potassium By similarity
Metal binding1651Potassium; via carbonyl oxygen By similarity
Metal binding3161Magnesium Potential
Metal binding3401Magnesium By similarity
Binding site1291Substrate By similarity
Binding site3391Substrate; via amide nitrogen By similarity
Binding site3401Substrate; via amide nitrogen By similarity
Binding site3721Substrate By similarity
Site3141Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93Z53 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4C61979F639274B1

FASTA57162,615
        10         20         30         40         50         60 
MAAYGQISSG MTVDPQVLSS SRNIGVSLSP LRRTLIGAGV RSTSISLRQC SLSVRSIKIS 

        70         80         90        100        110        120 
EDSRKPKAYA ENGAFDVGVL DSSSYRLADS RTSSNDSRRK TKIVCTIGPS SSSREMIWKL 

       130        140        150        160        170        180 
AEAGMNVARL NMSHGDHASH QITIDLVKEY NSLFVDKAIA IMLDTKGPEV RSGDVPQPIF 

       190        200        210        220        230        240 
LEEGQEFNFT IKRGVSLKDT VSVNYDDFVN DVEVGDILLV DGGMMSLAVK SKTSDLVKCV 

       250        260        270        280        290        300 
VIDGGELQSR RHLNVRGKSA TLPSITDKDW EDIKFGVDNQ VDFYAVSFVK DAKVVHELKN 

       310        320        330        340        350        360 
YLKTCSADIS VIVKIESADS IKNLPSIISA CDGAMVARGD LGAELPIEEV PLLQEEIIRR 

       370        380        390        400        410        420 
CRSIHKPVIV ATNMLESMIN HPTPTRAEVS DIAIAVREGA DAIMLSGETA HGKFPLKAVN 

       430        440        450        460        470        480 
VMHTVALRTE ASLPVRTSAS RTTAYKGHMG QMFAFHASIM ANTLSSPLIV FTRTGSMAVL 

       490        500        510        520        530        540 
LSHYRPSATI FAFTNQRRIM QRLALYQGVM PIYMEFSDDA EDTYARSLKL LQDENMLKEG 

       550        560        570 
QHVTLVQSGS QPIWREESTH LIQVRKIKIG G 

« Hide

References

« Hide 'large scale' references
[1]"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.
[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. 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.
[4]"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: TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY.
[5]"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: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
Strain: cv. Wassilewskija.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007767 Genomic DNA. Translation: AAF81342.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31487.1.
AY058121 mRNA. Translation: AAL25538.1.
BT001147 mRNA. Translation: AAN64538.1.
PIRF86449.
RefSeqNP_564402.1. NM_102979.1.
UniGeneAt.66798.

3D structure databases

ProteinModelPortalQ93Z53.
SMRQ93Z53. Positions 99-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G32440.1-P.

Proteomic databases

PaxDbQ93Z53.
PRIDEQ93Z53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G32440.1; AT1G32440.1; AT1G32440.
GeneID840138.
KEGGath:AT1G32440.

Organism-specific databases

TAIRAT1G32440.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021559.
InParanoidQ93Z53.
KOK00873.
OMAQRPEDIH.
PhylomeDBQ93Z53.

Enzyme and pathway databases

SABIO-RKQ93Z53.
UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorQ93Z53.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. 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]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKP3_ARATH
AccessionPrimary (citable) accession number: Q93Z53
Secondary accession number(s): Q9LQL3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 98 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