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Protein

Plastidial pyruvate kinase 4, chloroplastic

Gene

PKP4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathway:iglycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic (GAPC2), Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (GAPC1)
  2. no protein annotated in this organism
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (At3g08590), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (PGM1)
  4. Enolase (At2g36530), Enolase 1, chloroplastic (ENO1), Cytosolic enolase 3 (ENO3), Enolase, Bifunctional enolase 2/transcriptional activator (ENO2)
  5. Pyruvate kinase (At5g08570), Pyruvate kinase (At5g56350), Pyruvate kinase (F1I16_60), Pyruvate kinase (At3g25960), Pyruvate kinase (At5g63680), Plastidial pyruvate kinase 3, chloroplastic (PKP3), Pyruvate kinase (At3g52990), Pyruvate kinase (At2g36580), Pyruvate kinase, Probable pyruvate kinase, cytosolic isozyme (At4g26390), Pyruvate kinase (F8J2_160), Pyruvate kinase (At3g52990), Plastidial pyruvate kinase 2 (PKP2), Pyruvate kinase (T11I18.16), Pyruvate kinase (F1I16_220), Plastidial pyruvate kinase 1, chloroplastic (PKP1), Pyruvate kinase (At5g63680), Pyruvate kinase, Plastidial pyruvate kinase 4, chloroplastic (PKP4)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651SubstrateBy similarity
Metal bindingi267 – 2671PotassiumBy similarity
Metal bindingi299 – 2991PotassiumBy similarity
Sitei583 – 5831Transition state stabilizerBy similarity
Metal bindingi585 – 5851MagnesiumSequence Analysis
Binding sitei614 – 6141Substrate; via amide nitrogenBy similarity
Metal bindingi615 – 6151MagnesiumBy similarity
Binding sitei615 – 6151Substrate; via amide nitrogenBy similarity
Binding sitei647 – 6471SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BioCyciARA:AT3G49160-MONOMER.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Plastidial pyruvate kinase 4, chloroplastic (EC:2.7.1.40)
Short name:
PKp4
Gene namesi
Name:PKP4
Ordered Locus Names:At3g49160
ORF Names:F2K15.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G49160.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 710Plastidial pyruvate kinase 4, chloroplasticPRO_0000416990
Transit peptidei1 – ?ChloroplastSequence Analysis

Proteomic databases

PaxDbiQ9M3B6.
PRIDEiQ9M3B6.

Interactioni

Protein-protein interaction databases

BioGridi9395. 8 interactions.
IntActiQ9M3B6. 7 interactions.
STRINGi3702.AT3G49160.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M3B6.
SMRiQ9M3B6. Positions 233-362, 437-694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000224464.
InParanoidiQ9M3B6.
KOiK00873.
OMAiPCRILMD.
PhylomeDBiQ9M3B6.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 2 hits.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9M3B6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGLDSSHLL RDKILCFSSR SHINNQHKKT SYALSLNHMK LPIQRTLAFA
60 70 80 90 100
LARGKGEAES FSRLEATFGD NTSTECTWSF DFPDSKDAMS HLKSEADLSG
110 120 130 140 150
SNGANNVASV IEKLNALRSH LLAAEKWNAS QLHLCDSKYL ECATNLVHYM
160 170 180 190 200
ALRSLDIEQL NSHLASLGLS SLDNNNLDVL AHLNASINLL MNDQNAVTES
210 220 230 240 250
WTNVYPKGKS TKKNDKGRVL SYKESLLGKL REGRSTHIMV TIGEEATLSE
260 270 280 290 300
TFITDILKAG TSVIRINCAH GDPSIWGEII KRVRRTSQML EMPCRVHMDL
310 320 330 340 350
AGPKLRTGTL KPGPCVMKIS PKKDAYGNVV SPALVWLCLT GTEPPAHVSP
360 370 380 390 400
DATISVQGQD FLAGLQIGDS IRLCDARGRK RRLKISKEFH VFNSTGFVAE
410 420 430 440 450
CFDTAYIESG TELSVKGKKG RRLVGRVVDV PPKESFVRLK VGDLLVITRE
460 470 480 490 500
GSLDEPSVTV PGAHRLTCPS GYLFDSVKPG ETIGFDDGKI WGVIKGTSPS
510 520 530 540 550
EVIVSITHAR PKGTKLGSEK SINIPQSDIH FKGLTSKDIK DLDYVASHAD
560 570 580 590 600
MVGISFIRDV HDITVLRQEL KKRKLDDLGI VLKIETKSGF KNLSLILLEA
610 620 630 640 650
MKCSNPLGIM IARGDLAVEC GWERLANMQE EIIAICKAAR VPVIMATQVL
660 670 680 690 700
ESLVKSGVPT RAEITDAANA KRASCVMLNK GKNIVEAVSM LDTILHTKLI
710
YKKSDSENLH
Length:710
Mass (Da):77,827
Last modified:October 1, 2000 - v1
Checksum:i515D788AD6609E70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132956 Genomic DNA. Translation: CAB66395.1.
CP002686 Genomic DNA. Translation: AEE78506.1.
AY072177 mRNA. Translation: AAL59999.1.
AY096527 mRNA. Translation: AAM20177.1.
PIRiT45821.
RefSeqiNP_190485.1. NM_114775.2.
UniGeneiAt.35642.

Genome annotation databases

EnsemblPlantsiAT3G49160.1; AT3G49160.1; AT3G49160.
GeneIDi824077.
KEGGiath:AT3G49160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132956 Genomic DNA. Translation: CAB66395.1.
CP002686 Genomic DNA. Translation: AEE78506.1.
AY072177 mRNA. Translation: AAL59999.1.
AY096527 mRNA. Translation: AAM20177.1.
PIRiT45821.
RefSeqiNP_190485.1. NM_114775.2.
UniGeneiAt.35642.

3D structure databases

ProteinModelPortaliQ9M3B6.
SMRiQ9M3B6. Positions 233-362, 437-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9395. 8 interactions.
IntActiQ9M3B6. 7 interactions.
STRINGi3702.AT3G49160.1.

Proteomic databases

PaxDbiQ9M3B6.
PRIDEiQ9M3B6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G49160.1; AT3G49160.1; AT3G49160.
GeneIDi824077.
KEGGiath:AT3G49160.

Organism-specific databases

TAIRiAT3G49160.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000224464.
InParanoidiQ9M3B6.
KOiK00873.
OMAiPCRILMD.
PhylomeDBiQ9M3B6.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciARA:AT3G49160-MONOMER.

Miscellaneous databases

PROiQ9M3B6.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 2 hits.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiPKP4_ARATH
AccessioniPrimary (citable) accession number: Q9M3B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.