KPYC_SOYBN
ID KPYC_SOYBN Reviewed; 511 AA.
AC Q42806;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pyruvate kinase, cytosolic isozyme;
DE Short=PK;
DE EC=2.7.1.40;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8278551; DOI=10.1104/pp.102.4.1345;
RA Ma H., McMullen M.D., Finer J.J.;
RT "A pyruvate kinase cDNA from soybean somatic embryos.";
RL Plant Physiol. 102:1345-1345(1993).
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: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; L08632; AAA17000.1; -; mRNA.
DR PIR; T07787; T07787.
DR RefSeq; NP_001237968.1; NM_001251039.1.
DR AlphaFoldDB; Q42806; -.
DR SMR; Q42806; -.
DR STRING; 3847.GLYMA05G09310.2; -.
DR PRIDE; Q42806; -.
DR ProMEX; Q42806; -.
DR EnsemblPlants; KRH56499; KRH56499; GLYMA_05G000700.
DR EnsemblPlants; KRH56500; KRH56500; GLYMA_05G000700.
DR GeneID; 547791; -.
DR Gramene; KRH56499; KRH56499; GLYMA_05G000700.
DR Gramene; KRH56500; KRH56500; GLYMA_05G000700.
DR KEGG; gmx:547791; -.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; Q42806; -.
DR OMA; PGCHCAV; -.
DR OrthoDB; 933620at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000008827; Chromosome 5.
DR Genevisible; Q42806; GM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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 CDD; cd00288; Pyruvate_Kinase; 1.
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; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..511
FT /note="Pyruvate kinase, cytosolic isozyme"
FT /id="PRO_0000112125"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 53
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 241
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 55302 MW; BF0C06DAC6FD95F1 CRC64;
MANIDIEGIL KQQQPYDGRV PKTKIVCTLG PASRSVEMTE KLLRAGMNVA RFNFSHGTHD
YHQETLNNLK TAMHNTGILC AVMLDTKGPE IRTGFLKDGK PIQLKEGQEV TITTDYDIKG
DPEMISMSYK KLPVHLKPGN TILCSDGTIT LTVLSCDPDA GTVRCRCENT ATLGERKNVN
LPGVVVDLPT LTEKDKEDIL GWGVPNKIDM IALSFVRKGS DLVNVRKVLG PHAKNIQLMS
KVENQEGVLN FDEILRETDA FMVARGDLGM EIPVEKIFLA QKMMIYKCNL VGKPVVTATQ
MLESMIKSPR PTRAEATDVA NAVLDGTDCV MLSGESAAGA YPELAVKIMA RICIEAESSL
DYGAIFKEMI RSTPLPMSPL ESLASSAVRT ANKAKAKLIV VLTRGGSTAK LVAKYRPAVP
ILSVVVPVLS TDSFDWTCSD ETPARHSLIY RGLIPILGEG SAKATDAEST EVILEAALKS
ATERALCKPG DAVVALHRIG AASVIKICIV K
