KPYA_RICCO
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 03-AUG-2022, entry version 121.
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}.
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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. [Q43117-1]
DR AlphaFoldDB; Q43117; -.
DR SMR; Q43117; -.
DR STRING; 3988.XP_002517044.1; -.
DR PRIDE; Q43117; -.
DR GeneID; 8280200; -.
DR KEGG; rcu:8280200; -.
DR eggNOG; KOG2323; Eukaryota.
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 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 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
