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   27-MAR-2024, entry version 154.
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;
GN   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.Q9FLW9; -.
DR   iPTMnet; Q9FLW9; -.
DR   PaxDb; 3702-AT5G52920-1; -.
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; AT5G52920; PKP-BETA1.
DR   eggNOG; KOG2323; Eukaryota.
DR   HOGENOM; CLU_015439_3_2_1; -.
DR   InParanoid; Q9FLW9; -.
DR   OMA; NEQLAHV; -.
DR   OrthoDB; 601at2759; -.
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   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
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:0006629; P:lipid metabolic process; IGI:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048316; P:seed development; IMP:TAIR.
DR   GO; GO:0010431; P:seed maturation; IMP:UniProtKB.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF2; PLASTIDIAL PYRUVATE KINASE 2; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR   Genevisible; Q9FLW9; AT.
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
//