KPYA_TOBAC
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 03-AUG-2022, entry version 112.
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}.
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DR EMBL; Z28373; CAA82222.1; -; mRNA.
DR PIR; S51946; S51946.
DR AlphaFoldDB; Q40545; -.
DR SMR; Q40545; -.
DR STRING; 4097.Q40545; -.
DR PRIDE; 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 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 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
