ID KPYA_TOBAC Reviewed; 593 AA. AC Q40545; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 08-NOV-2023, entry version 119. DE RecName: Full=Pyruvate kinase isozyme A, chloroplastic; DE EC=2.7.1.40; DE Flags: Precursor; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Petit Havana SR1; TISSUE=Seed; RX PubMed=7865798; DOI=10.1007/bf00019180; RA Blakeley S.D., Gottlob-Mchugh S., Wan J., Crews L., Miki B., Ko K., RA Dennis D.T.; RT "Molecular characterization of plastid pyruvate kinase from castor and RT tobacco."; RL Plant Mol. Biol. 27:79-89(1995). 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- TISSUE SPECIFICITY: Highest levels in roots. Also found in stems, CC leaves and flowers. CC -!- DEVELOPMENTAL STAGE: Most abundantly expressed during the early CC globular to early cotyledonary stages of embryo development. 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; Z28373; CAA82222.1; -; mRNA. DR PIR; S51946; S51946. DR AlphaFoldDB; Q40545; -. DR SMR; Q40545; -. DR STRING; 4097.Q40545; -. DR PaxDb; 4097-Q40545; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000084051; Unplaced. DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central. 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; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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 2: Evidence at transcript 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..? FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN ?..593 FT /note="Pyruvate kinase isozyme A, chloroplastic" FT /id="PRO_0000016663" FT REGION 57..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 146..149 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 146 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 179 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 343 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255" FT BINDING 366 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 367 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 367 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 399 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 341 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 593 AA; 65228 MW; FAF049E193C1D484 CRC64; MSQALNFFVS SSSRSPATFT ISRPSVFPST GSLRLLVKKS LRTLVVEASS AAASDLDEPQ SSPVLVSENG SGGVLSSATQ EYGRNAAPGT DSSSIEVDTV TEAELKENGF RSTRRTKLIC TIGPATCGFE QLERLAEGGM NVARINMCHG TREWHRMVIE RLRRLNEEKG FAVAIMMDTE GSEIHMGDLG GASSAKAEDG EIWNFTVRSF DPPLPERTVT VNYDGFAEDV KVGDELLVDG GMVRFEVIEK IGPDVKCLCT DPGLLLPRAN LTFWRDGKLV RERNAMLPTI SSKDWLDIDF GIAEGVDFIA VSFVKSAEVI KHLKSYIQAR ARDSDISVIA KIESIDSLKN LEEIIQASDG AMVARGDLGA QIPLEQVPSE QQKIVQICRQ LNRPVIVASQ LLESMIEYPI PTRAEVADVS EAVRQRGDAL MLSGESAMGQ FPEKALTVLR SVSLRIERMW REQKRHEVIE LPSIASSFSD SISEEICNSA AKMANNLEVD ALFVYTKNGH MASLLSRCRP DCPIFAFTTT TSVRRRLNLQ WGLMPFRLSF SDDMESNLNK TFSLLKARGM IKSGDLIIAV SDMLQSIQVM NVP //