PKP1_ARATH
ID PKP1_ARATH Reviewed; 596 AA.
AC Q9LIK0; Q8LEY6; Q93ZY0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Plastidial pyruvate kinase 1, chloroplastic;
DE Short=PK1;
DE Short=PKp1;
DE EC=2.7.1.40;
DE AltName: Full=Pyruvate kinase II;
DE AltName: Full=Pyruvate kinase isozyme A;
DE Short=PKP-ALPHA;
DE Flags: Precursor;
GN Name=PKP1; Synonyms=PK1; OrderedLocusNames=At3g22960; ORFNames=F5N5.15;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, COFACTOR,
RP 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 [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [9]
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:17892448,
CC 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 7.8-8.2. {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:17557808, ECO:0000269|PubMed:17892448,
CC ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower extent,
CC in roots, leaves (veins and trichomes), stems, inflorescences,
CC siliques, 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:17892448,
CC ECO:0000269|PubMed:17965177}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; AP001300; BAB03043.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76697.1; -; Genomic_DNA.
DR EMBL; AY056196; AAL07045.2; -; mRNA.
DR EMBL; AY056793; AAL10484.1; -; mRNA.
DR EMBL; AY058084; AAL24192.1; -; mRNA.
DR EMBL; BT002329; AAN86162.1; -; mRNA.
DR EMBL; AY085149; AAM61702.1; -; mRNA.
DR RefSeq; NP_566720.1; NM_113196.3.
DR AlphaFoldDB; Q9LIK0; -.
DR SMR; Q9LIK0; -.
DR BioGRID; 7202; 35.
DR IntAct; Q9LIK0; 30.
DR STRING; 3702.AT3G22960.1; -.
DR iPTMnet; Q9LIK0; -.
DR PaxDb; Q9LIK0; -.
DR PRIDE; Q9LIK0; -.
DR ProteomicsDB; 234963; -.
DR EnsemblPlants; AT3G22960.1; AT3G22960.1; AT3G22960.
DR GeneID; 821870; -.
DR Gramene; AT3G22960.1; AT3G22960.1; AT3G22960.
DR KEGG; ath:AT3G22960; -.
DR Araport; AT3G22960; -.
DR TAIR; locus:2084583; AT3G22960.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_3_0_1; -.
DR InParanoid; Q9LIK0; -.
DR OMA; QHTINVN; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; Q9LIK0; -.
DR SABIO-RK; Q9LIK0; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:Q9LIK0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIK0; baseline and differential.
DR Genevisible; Q9LIK0; 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: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:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IGI: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 Nucleotide-binding; Plastid; Potassium; Pyruvate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 88..596
FT /note="Plastidial pyruvate kinase 1, chloroplastic"
FT /id="PRO_0000416987"
FT REGION 47..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 149
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 182
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 344
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT CONFLICT 9
FT /note="T -> S (in Ref. 4; AAM61702)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> P (in Ref. 4; AAM61702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 65131 MW; 256CE329639A4BFD CRC64;
MSQSIQFSTP SHTPHLLHLP HSQFNRPLSS ISFRRFPLTT IKYTSIRASS SSSPSPDLDS
SSSSSSSQVL LSPNGTGAVK SDERSVVATA VTTDTSGIEV DTVTEAELKE NGFRSTRRTK
LICTIGPATC GFEQLEALAV GGMNVARLNM CHGTRDWHRG VIRSVRRLNE EKGFAVAIMM
DTEGSEIHMG DLGGEASAKA EDGEVWTFTV RAFDSSRPER TISVSYDGFA EDVRVGDELL
VDGGMVRFEV IEKIGPDVKC LCTDPGLLLP RANLTFWRDG SLVRERNAML PTISSKDWLD
IDFGIAEGVD FIAVSFVKSA EVINHLKSYL AARSRGGEIG VIAKIESIDS LTNLEEIILA
SDGAMVARGD LGAQIPLEQV PAAQQRIVQV CRALNKPVIV ASQLLESMIE YPTPTRAEVA
DVSEAVRQRS DALMLSGESA MGQFPDKALT VLRTVSLRIE RWWREEKRHE SVPLQAIGSS
FSDKISEEIC NSAAKMANNL GVDAVFVYTT SGHMASLVSR CRPDCPIFAF TTTTSVRRRL
NLQWGLIPFR LSFSDDMESN LNKTFSLLKS RGMIKSGDLV IAVSDMLQSI QVMNVP
