PKP3_ARATH
ID PKP3_ARATH Reviewed; 571 AA.
AC Q93Z53; Q9LQL3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Plastidial pyruvate kinase 3, chloroplastic;
DE Short=PKp3;
DE EC=2.7.1.40;
DE AltName: Full=Pyruvate kinase I;
DE AltName: Full=Pyruvate kinase isozyme B2, chloroplastic;
DE Short=PKP-BETA2;
DE Short=Plastidic pyruvate kinase beta subunit 2;
DE Flags: Precursor;
GN Name=PKP3; OrderedLocusNames=At1g32440; ORFNames=F5D14.22;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, 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 [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=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 [6]
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.
CC {ECO:0000250}.
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 -!- 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:18431481}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves,
CC inflorescences, siliques, pollen, seeds and flowers.
CC {ECO:0000269|PubMed:17557808, ECO:0000269|PubMed:17892448}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81342.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007767; AAF81342.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31487.1; -; Genomic_DNA.
DR EMBL; AY058121; AAL25538.1; -; mRNA.
DR EMBL; BT001147; AAN64538.1; -; mRNA.
DR PIR; F86449; F86449.
DR RefSeq; NP_564402.1; NM_102979.2.
DR AlphaFoldDB; Q93Z53; -.
DR SMR; Q93Z53; -.
DR BioGRID; 25372; 1.
DR STRING; 3702.AT1G32440.1; -.
DR PaxDb; Q93Z53; -.
DR PRIDE; Q93Z53; -.
DR ProteomicsDB; 234763; -.
DR EnsemblPlants; AT1G32440.1; AT1G32440.1; AT1G32440.
DR GeneID; 840138; -.
DR Gramene; AT1G32440.1; AT1G32440.1; AT1G32440.
DR KEGG; ath:AT1G32440; -.
DR Araport; AT1G32440; -.
DR TAIR; locus:2033760; AT1G32440.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_2_1; -.
DR InParanoid; Q93Z53; -.
DR OMA; GHMGEMF; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; Q93Z53; -.
DR SABIO-RK; Q93Z53; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:Q93Z53; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Z53; baseline and differential.
DR Genevisible; Q93Z53; AT.
DR GO; GO:0009507; C:chloroplast; HDA: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:0010431; P:seed maturation; ISS: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..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..571
FT /note="Plastidial pyruvate kinase 3, chloroplastic"
FT /id="PRO_0000416989"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 131..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 131
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 133
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 164
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 165
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 314
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
SQ SEQUENCE 571 AA; 62615 MW; 4C61979F639274B1 CRC64;
MAAYGQISSG MTVDPQVLSS SRNIGVSLSP LRRTLIGAGV RSTSISLRQC SLSVRSIKIS
EDSRKPKAYA ENGAFDVGVL DSSSYRLADS RTSSNDSRRK TKIVCTIGPS SSSREMIWKL
AEAGMNVARL NMSHGDHASH QITIDLVKEY NSLFVDKAIA IMLDTKGPEV RSGDVPQPIF
LEEGQEFNFT IKRGVSLKDT VSVNYDDFVN DVEVGDILLV DGGMMSLAVK SKTSDLVKCV
VIDGGELQSR RHLNVRGKSA TLPSITDKDW EDIKFGVDNQ VDFYAVSFVK DAKVVHELKN
YLKTCSADIS VIVKIESADS IKNLPSIISA CDGAMVARGD LGAELPIEEV PLLQEEIIRR
CRSIHKPVIV ATNMLESMIN HPTPTRAEVS DIAIAVREGA DAIMLSGETA HGKFPLKAVN
VMHTVALRTE ASLPVRTSAS RTTAYKGHMG QMFAFHASIM ANTLSSPLIV FTRTGSMAVL
LSHYRPSATI FAFTNQRRIM QRLALYQGVM PIYMEFSDDA EDTYARSLKL LQDENMLKEG
QHVTLVQSGS QPIWREESTH LIQVRKIKIG G
