ID KPYA_RICCO Reviewed; 583 AA. AC Q43117; Q43118; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 128. DE RecName: Full=Pyruvate kinase isozyme A, chloroplastic; DE EC=2.7.1.40; DE Flags: Precursor; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae; OC Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND PROTEIN SEQUENCE RP OF 75-81. RC STRAIN=cv. Baker 296; TISSUE=Endosperm; RX PubMed=16668331; DOI=10.1104/pp.96.4.1283; RA Blakeley S.D., Plaxton W.C., Dennis D.T.; RT "Relationship between the subunits of leucoplast pyruvate kinase from RT Ricinus communis and a comparison with the enzyme from other sources."; RL Plant Physiol. 96:1283-1288(1991). 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; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Oligomer of alpha and beta subunits. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Alpha; CC IsoId=Q43117-1; Sequence=Displayed; CC Name=Beta; CC IsoId=Q43117-2; Sequence=VSP_002886; CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M64736; AAA33870.1; -; mRNA. DR EMBL; M64737; AAA33871.1; -; mRNA. DR PIR; T10051; T10051. DR PIR; T10054; T10054. DR RefSeq; XP_002517044.1; XM_002516998.2. DR AlphaFoldDB; Q43117; -. DR SMR; Q43117; -. DR eggNOG; KOG2323; Eukaryota. DR OrthoDB; 599465at2759; -. DR SABIO-RK; Q43117; -. DR UniPathway; UPA00109; UER00188. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:SF14; PLASTIDIAL PYRUVATE KINASE 1, CHLOROPLASTIC; 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. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Chloroplast; Direct protein sequencing; KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Plastid; KW Potassium; Pyruvate; Transferase; Transit peptide. FT TRANSIT 1..74 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:16668331" FT CHAIN 75..583 FT /note="Pyruvate kinase isozyme A, chloroplastic" FT /id="PRO_0000016662" FT REGION 43..75 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 136..139 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 136 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 168 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 333 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255" FT BINDING 356 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 389 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 331 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT VAR_SEQ 1..129 FT /note="MSQSLHFSPNLTFAKQPFPKLPLPFPTSNSRYPVNNYKSLSIKASTSPSSSS FT DPQVLVADNGTGNSGVLYNNNNKSVTVSDPSSIEVDAVTETELKENGFRSTRRTKLVCT FT IGPATCGFEELEALAVGG -> MAVVVKDLEEAVRVVVLAVLRDMEVVVVLVTAVMGVV FT GD (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:16668331" FT /id="VSP_002886" SQ SEQUENCE 583 AA; 64094 MW; 5DFDE4F778A753C2 CRC64; MSQSLHFSPN LTFAKQPFPK LPLPFPTSNS RYPVNNYKSL SIKASTSPSS SSDPQVLVAD NGTGNSGVLY NNNNKSVTVS DPSSIEVDAV TETELKENGF RSTRRTKLVC TIGPATCGFE ELEALAVGGM NVARINMCHG TREWHKSVIE RVRRLNEEKG FAVAIMMDTE GSEIHMGDLG GASSAKAEDG EIWTFSVRAY DSPRPERTIN VNYDGFAEDV KVGDELLVDG GMVRFEVIEK IGPDVKCRCT DPGLLLPRAN LTFWRDGSLV RERNAMLPTI SSKDWLDIDF GIAEGVDFIA ISFVKSAEVI NHLKSYIAAR SRDSDIAVIA KIESIDSLKN LEEIIRASDG AMVARGDLGA QIPLEQVPSA QQNIVQVCRQ LNKPVIVASQ LLESMIEYPT PTRAEVADVS EAVRQRADAL MLSGESAMGQ YPEKALAVLR SVSVRIEKWW REEKHHEAME LPAIGSTYSD SISEEICNSA AKMANNLGVD ALFVYTKDGH MASLLSRCRP DCPIFAFTTT TSVRRRLNLQ WGLIPFRLSF ADDMESNLNK TFSLLKARGM IKSGDLVIAV SDMLQSIQVM NVP //