ID   KPYC2_ORYSI             Reviewed;         527 AA.
AC   B8BM17;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Pyruvate kinase 2, cytosolic {ECO:0000305};
DE            Short=OsPK2 {ECO:0000305};
DE            EC=2.7.1.40 {ECO:0000305};
GN   ORFNames=OsI_37456 {ECO:0000312|EMBL:EEC68859.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Key regulatory enzyme of the glycolytic pathway that
CC       catalyzes the final step of glycolysis, converting ADP and
CC       phosphoenolpyruvate (PEP) to ATP and pyruvate by essentially
CC       irreversible transphosphorylation. {ECO:0000250|UniProtKB:Q2RAK2}.
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; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P30613}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q2RAK2}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; CM000137; EEC68859.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BM17; -.
DR   SMR; B8BM17; -.
DR   STRING; 39946.B8BM17; -.
DR   iPTMnet; B8BM17; -.
DR   EnsemblPlants; BGIOSGA036640-TA; BGIOSGA036640-PA; BGIOSGA036640.
DR   Gramene; BGIOSGA036640-TA; BGIOSGA036640-PA; BGIOSGA036640.
DR   HOGENOM; CLU_015439_9_1_1; -.
DR   OMA; NDVVCII; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000007015; Chromosome 12.
DR   GO; GO:0005829; C:cytosol; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..527
FT                   /note="Pyruvate kinase 2, cytosolic"
FT                   /id="PRO_0000433958"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         60..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         60
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         62
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         92
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         93
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   SITE            256
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00549"
SQ   SEQUENCE   527 AA;  57442 MW;  601F36307ADA741B CRC64;
     MHSTNLLLEE PIRMASILEP SKPSFFPAMT KIVGTLGPKS RSVDTISSCL KAGMSVARFD
     FSWGDAEYHQ ETLENLKVAI KSTKKLCAVM LDTVGPELQV VNKSEASISL EENGTVILTP
     DQGQEASSQV LPINFAGLAK AVKPGDTIFV GQYLFTGSET TSVWLEVSQI KGDDVVCVIK
     NTATLAGSLF TLHCSQIHID LPTLSDEDKE VIRKWGAPNK IDFLSLSYTR HVEDVRQARE
     FLSKLGDLSQ TQIFAKIENV EGLNNFDEIL QEADGIILSR GNLGIDLPPE KVFLFQKSAL
     HKCNMAGKPA VVTRVVDSMT DNLRPTRAEA TDVANAVLDG SDAILLGAET LRGLYPVETI
     SIVGKICAEA EKVFNQDLYF KRTVKHVGEP MTHLESIASS AVRAAIKVKA SVIICFTSSG
     RAARLIAKYR PTMPVLSVVI PRLKTNQLRW SFTGAFEARQ SLIVRGLFPM LADPRHPAES
     TNATNESVLK VALDHGKVSG VIKSHDRVVV CQKVGDSSVV KIIELDD