PKP2_ARATH
ID PKP2_ARATH Reviewed; 579 AA.
AC Q9FLW9; Q56XD5; Q56ZT8; Q570A3; Q94AG4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Plastidial pyruvate kinase 2;
DE Short=PKp2;
DE EC=2.7.1.40;
DE AltName: Full=Plastidial pyruvate kinase 1;
DE Short=PKP1;
DE AltName: Full=Pyruvate kinase III;
DE AltName: Full=Pyruvate kinase isozyme B1, chloroplastic;
DE Short=PKP-BETA1;
DE Short=Plastidic pyruvate kinase beta subunit 1;
DE Flags: Precursor;
GN Name=PKP2; Synonyms=PKP1; OrderedLocusNames=At5g52920; ORFNames=MXC20.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=12953116; DOI=10.1105/tpc.012500;
RA Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
RA Leaver C.J., Sweetlove L.J.;
RT "Enzymes of glycolysis are functionally associated with the mitochondrion
RT in Arabidopsis cells.";
RL Plant Cell 15:2140-2151(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR
RP LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND GENE FAMILY.
RX PubMed=17557808; DOI=10.1105/tpc.106.048629;
RA Andre C., Froehlich J.E., Moll M.R., Benning C.;
RT "A heteromeric plastidic pyruvate kinase complex involved in seed oil
RT biosynthesis in Arabidopsis.";
RL Plant Cell 19:2006-2022(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17892448; DOI=10.1111/j.1365-313x.2007.03232.x;
RA Baud S., Wuilleme S., Dubreucq B., de Almeida A., Vuagnat C., Lepiniec L.,
RA Miquel M., Rochat C.;
RT "Function of plastidial pyruvate kinases in seeds of Arabidopsis
RT thaliana.";
RL Plant J. 52:405-419(2007).
RN [9]
RP FUNCTION.
RX PubMed=17965177; DOI=10.1104/pp.107.108340;
RA Andre C., Benning C.;
RT "Arabidopsis seedlings deficient in a plastidic pyruvate kinase are unable
RT to utilize seed storage compounds for germination and establishment.";
RL Plant Physiol. 145:1670-1680(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Required for plastidial pyruvate kinase activity. Involved in
CC seed oil accumulation, embryo development and seed storage compounds
CC mobilization upon germination. {ECO:0000269|PubMed:17557808,
CC ECO:0000269|PubMed:17892448, ECO:0000269|PubMed:17965177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17557808};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:17557808};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8-8.0. {ECO:0000269|PubMed:17557808,
CC ECO:0000269|PubMed:17892448};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Oligomer of alpha and beta subunits.
CC {ECO:0000269|PubMed:17557808}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}. Mitochondrion
CC {ECO:0000269|PubMed:12953116}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower extent,
CC in roots, leaves (veins and trichomes), inflorescences, siliques,
CC pollen (grains and tubes) and flowers (sepals and petals).
CC {ECO:0000269|PubMed:17557808, ECO:0000269|PubMed:17892448}.
CC -!- DEVELOPMENTAL STAGE: In seeds, accumulates in endosperm and embryo. In
CC torpedo-shaped embryos, restricted to the hypocotyl and in the outer
CC parts of the young cotyledons. In later embryo stages, present in all
CC tissues except root tips. {ECO:0000269|PubMed:17892448}.
CC -!- DISRUPTION PHENOTYPE: Reduced plastidial pyruvate kinase activity and
CC altered seed oil content leading to wrinkled seeds, retarded embryo
CC elongation and reduced seed germination. {ECO:0000269|PubMed:17557808,
CC ECO:0000269|PubMed:17892448}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; AB009055; BAB10440.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96278.1; -; Genomic_DNA.
DR EMBL; AY048198; AAK82461.1; -; mRNA.
DR EMBL; AY091682; AAM10281.1; -; mRNA.
DR EMBL; AK220807; BAD94078.1; -; mRNA.
DR EMBL; AK220873; BAD94256.1; -; mRNA.
DR EMBL; AK221740; BAD93771.1; -; mRNA.
DR EMBL; AY084507; AAM61075.1; -; mRNA.
DR RefSeq; NP_200104.1; NM_124670.3.
DR AlphaFoldDB; Q9FLW9; -.
DR SMR; Q9FLW9; -.
DR STRING; 3702.AT5G52920.1; -.
DR iPTMnet; Q9FLW9; -.
DR PaxDb; Q9FLW9; -.
DR PRIDE; Q9FLW9; -.
DR ProteomicsDB; 234915; -.
DR EnsemblPlants; AT5G52920.1; AT5G52920.1; AT5G52920.
DR GeneID; 835369; -.
DR Gramene; AT5G52920.1; AT5G52920.1; AT5G52920.
DR KEGG; ath:AT5G52920; -.
DR Araport; AT5G52920; -.
DR TAIR; locus:2176912; AT5G52920.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_3_2_1; -.
DR InParanoid; Q9FLW9; -.
DR OMA; WDKLHHL; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; Q9FLW9; -.
DR SABIO-RK; Q9FLW9; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:Q9FLW9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLW9; baseline and differential.
DR Genevisible; Q9FLW9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0004743; F:pyruvate kinase activity; IDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IGI:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0010431; P:seed maturation; IMP:UniProtKB.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Plastid; Potassium; Pyruvate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..579
FT /note="Plastidial pyruvate kinase 2"
FT /id="PRO_0000416988"
FT REGION 6..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 142..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 142
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 144
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 175
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 176
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 325
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT CONFLICT 342
FT /note="S -> P (in Ref. 3; AAK82461/AAM10281)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="T -> A (in Ref. 4; BAD93771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63522 MW; 9A728605C826B4D3 CRC64;
MAQVVATRSI QGSMLSPNGG SVSTRSEKLL KPASFAVKVL GNEAKRSGRV SVRSRRVVDT
TVRSARVETE VIPVSPEDVP NREEQLERLL EMQQFGDTSV GMWSKPTVRR KTKIVCTVGP
STNTREMIWK LAEAGMNVAR MNMSHGDHAS HKKVIDLVKE YNAQTKDNTI AIMLDTKGPE
VRSGDLPQPI MLDPGQEFTF TIERGVSTPS CVSVNYDDFV NDVEAGDMLL VDGGMMSFMV
KSKTKDSVKC EVVDGGELKS RRHLNVRGKS ATLPSITEKD WEDIKFGVEN KVDFYAVSFV
KDAQVVHELK KYLQNSGADI HVIVKIESAD SIPNLHSIIT ASDGAMVARG DLGAELPIEE
VPILQEEIIN LCRSMGKAVI VATNMLESMI VHPTPTRAEV SDIAIAVREG ADAVMLSGET
AHGKFPLKAA GVMHTVALRT EATITSGEMP PNLGQAFKNH MSEMFAYHAT MMSNTLGTST
VVFTRTGFMA ILLSHYRPSG TIYAFTNEKK IQQRLALYQG VCPIYMEFTD DAEETFANAL
ATLLKQGMVK KGEEIAIVQS GTQPIWRSQS THNIQVRKV
