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O65595 (KPYC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pyruvate kinase, cytosolic isozyme
Short name=PK
EC=2.7.1.40
Gene names
Ordered Locus Names:At4g26390
ORF Names:M3E9.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Pyruvate
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

potassium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Probable pyruvate kinase, cytosolic isozyme
PRO_0000112123

Sites

Metal binding391Potassium By similarity
Metal binding411Potassium By similarity
Metal binding711Potassium By similarity
Metal binding721Potassium; via carbonyl oxygen By similarity
Metal binding2291Magnesium By similarity
Metal binding2531Magnesium By similarity
Binding site371Substrate By similarity
Binding site2521Substrate; via amide nitrogen By similarity
Binding site2531Substrate; via amide nitrogen By similarity
Binding site2851Substrate By similarity
Site2271Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
O65595 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 45D43EF54A89FE62

FASTA49754,319
        10         20         30         40         50         60 
MAMEQRPKTK IVCTLGPASR SVPMVEKLLM AGMSVARFNF SHGSYEYHQE TLDNLRQAML 

        70         80         90        100        110        120 
NTGMLCAVML DTKGPEIRTG FLKDGKPIQL KQGQEITIST DYDLKGDEKT ICMSYKKLAQ 

       130        140        150        160        170        180 
DVNPGMVILC ADGTISLKVL SCDKEKGTVR CRCENTSMLG ERKNVNLPGV VVDLPTLTEK 

       190        200        210        220        230        240 
DKQDILEWGV PNQIDMIALS FVRKGSDLVQ VRKLLGKHAK TILLMSKVEN QEGVANFDDI 

       250        260        270        280        290        300 
LINSDAFMIA RGDLGMEIPI EKIFLAQKVM IYKCNFMGKP VVTATQMLES MIKSPRPTRA 

       310        320        330        340        350        360 
EATDVANAVL DGTDCVMLSG ETAAGAYPEL AVRTMAKICV EAESTLDYGD IFKRIMLHAA 

       370        380        390        400        410        420 
VPMSPMESLA SSAVRTATSS RATLMMVLTR GGSTARLVAK YRPGIPILSV VVPEITSDSF 

       430        440        450        460        470        480 
DWACSNEAPA RHSLIYRGLV PVLYAGSARA SIDESTEETL EFASEYGKKK QLCKTGDSVV 

       490 
ALFRTGNAIV IKILTVK

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL022223 Genomic DNA. Translation: CAA18231.1.
AL161565 Genomic DNA. Translation: CAB79494.1.
CP002687 Genomic DNA. Translation: AEE85192.1.
IPIIPI00544139.
PIRT05065.
RefSeqNP_194369.1. NM_118772.1.
UniGeneAt.54520.

3D structure databases

ProteinModelPortalO65595.
SMRO65595. Positions 8-482.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G26390.1-P.

Proteomic databases

PaxDbO65595.
PRIDEO65595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G26390.1; AT4G26390.1; AT4G26390.
GeneID828745.
KEGGath:AT4G26390.

Organism-specific databases

TAIRAt4g26390.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021559.
InParanoidO65595.
KOK00873.
OMACHHAQDE.
PhylomeDBO65595.
ProtClustDBPLN02461.

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorO65595.
GermOnlineAT4G26390. Arabidopsis thaliana.

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.
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. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYC_ARATH
AccessionPrimary (citable) accession number: O65595
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

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