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Q9M3B6 (PKP4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 93. 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 4, chloroplastic

Short name=PKp4
EC=2.7.1.40
Gene names
Name:PKP4
Ordered Locus Names:At3g49160
ORF Names:F2K15.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium By similarity.

Potassium By similarity.

Pathway

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

Subcellular location

Plastidchloroplast stroma By similarity.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   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_componentchloroplast stroma

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 710Plastidial pyruvate kinase 4, chloroplasticPRO_0000416990

Sites

Metal binding2671Potassium By similarity
Metal binding2991Potassium By similarity
Metal binding5851Magnesium Potential
Metal binding6151Magnesium By similarity
Binding site2651Substrate By similarity
Binding site6141Substrate; via amide nitrogen By similarity
Binding site6151Substrate; via amide nitrogen By similarity
Binding site6471Substrate By similarity
Site5831Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M3B6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 515D788AD6609E70

FASTA71077,827
        10         20         30         40         50         60 
MVGLDSSHLL RDKILCFSSR SHINNQHKKT SYALSLNHMK LPIQRTLAFA LARGKGEAES 

        70         80         90        100        110        120 
FSRLEATFGD NTSTECTWSF DFPDSKDAMS HLKSEADLSG SNGANNVASV IEKLNALRSH 

       130        140        150        160        170        180 
LLAAEKWNAS QLHLCDSKYL ECATNLVHYM ALRSLDIEQL NSHLASLGLS SLDNNNLDVL 

       190        200        210        220        230        240 
AHLNASINLL MNDQNAVTES WTNVYPKGKS TKKNDKGRVL SYKESLLGKL REGRSTHIMV 

       250        260        270        280        290        300 
TIGEEATLSE TFITDILKAG TSVIRINCAH GDPSIWGEII KRVRRTSQML EMPCRVHMDL 

       310        320        330        340        350        360 
AGPKLRTGTL KPGPCVMKIS PKKDAYGNVV SPALVWLCLT GTEPPAHVSP DATISVQGQD 

       370        380        390        400        410        420 
FLAGLQIGDS IRLCDARGRK RRLKISKEFH VFNSTGFVAE CFDTAYIESG TELSVKGKKG 

       430        440        450        460        470        480 
RRLVGRVVDV PPKESFVRLK VGDLLVITRE GSLDEPSVTV PGAHRLTCPS GYLFDSVKPG 

       490        500        510        520        530        540 
ETIGFDDGKI WGVIKGTSPS EVIVSITHAR PKGTKLGSEK SINIPQSDIH FKGLTSKDIK 

       550        560        570        580        590        600 
DLDYVASHAD MVGISFIRDV HDITVLRQEL KKRKLDDLGI VLKIETKSGF KNLSLILLEA 

       610        620        630        640        650        660 
MKCSNPLGIM IARGDLAVEC GWERLANMQE EIIAICKAAR VPVIMATQVL ESLVKSGVPT 

       670        680        690        700        710 
RAEITDAANA KRASCVMLNK GKNIVEAVSM LDTILHTKLI YKKSDSENLH 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(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: GENE FAMILY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL132956 Genomic DNA. Translation: CAB66395.1.
CP002686 Genomic DNA. Translation: AEE78506.1.
AY072177 mRNA. Translation: AAL59999.1.
AY096527 mRNA. Translation: AAM20177.1.
PIRT45821.
RefSeqNP_190485.1. NM_114775.2.
UniGeneAt.35642.

3D structure databases

ProteinModelPortalQ9M3B6.
SMRQ9M3B6. Positions 228-702.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9M3B6. 7 interactions.
STRING3702.AT3G49160.1-P.

Proteomic databases

PaxDbQ9M3B6.
PRIDEQ9M3B6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G49160.1; AT3G49160.1; AT3G49160.
GeneID824077.
KEGGath:AT3G49160.

Organism-specific databases

TAIRAT3G49160.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000224464.
InParanoidQ9M3B6.
KOK00873.
OMAAFRINCA.
PhylomeDBQ9M3B6.
ProtClustDBCLSN2684230.

Enzyme and pathway databases

BioCycARA:AT3G49160-MONOMER.
UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorQ9M3B6.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015793. Pyrv_Knase_brl.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 2 hits.
[Graphical view]
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
ProtoNetSearch...

Entry information

Entry namePKP4_ARATH
AccessionPrimary (citable) accession number: Q9M3B6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 93 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