KPYK_AGABI
ID KPYK_AGABI Reviewed; 532 AA.
AC O94122; Q9UVX2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pkiA;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Horst H39;
RA Schaap P.J., Mueller Y., van Griensven L.J.L.D., Visser J.;
RT "Sequence of the Agaricus bisporus pkiA gene.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE OF 3-532.
RC STRAIN=Horst U1;
RX AGRICOLA=IND21972038;
RA De Groot P.W.J., Visser J., van Griensven L.J.L.D., Schaap P.J.;
RT "Biochemical and molecular aspects of growth on fruiting of the edible
RT mushroom Agaricus bisporus.";
RL Mycol. Res. 102:1297-1308(1998).
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 -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; X97579; CAA66194.1; -; Genomic_DNA.
DR EMBL; X91106; CAA62560.1; -; mRNA.
DR AlphaFoldDB; O94122; -.
DR SMR; O94122; -.
DR PRIDE; O94122; -.
DR UniPathway; UPA00109; UER00188.
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 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; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..532
FT /note="Pyruvate kinase"
FT /id="PRO_0000112106"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 65
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 254
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 532 AA; 58249 MW; 3D569B9A2639CDE6 CRC64;
MYPVDGIRSQ IEWNTTLNVS DAPVPTETTK YHRKTAIIAT IGPKINTVEK LTDVRLAGVN
IVRMNFSHGT HEYHQSVIDN TRQMIKNDPH GRPVAIALDT KGPEIRTGQT RDGNDYPIKA
GDEFIVTTDP KYSDICDNKV LFVDYANLAS VTAPGKLIYI DDGIISLLIL SIDGMNLHVR
ALNNGTLSSR KGVNLPKTDV DLPPLSEKDK DDLRFGIRNG VDMIFASFIR RGEDVRQIRE
VLGPDGASIK IIVKIENEQG VANFDEILKE ADGVMVARGD LGIEIPASQV FLAQKMMIAK
CNIVGKPVIV ATQMLESMTY NPRPTRAEVS DVANAVLDGS DCVMLSGETA KGSYPVQSVL
MMAETCLLAE TAICYPPLYD DLRAVQARPT ETAETVAIAA VAAAAEQDAK ALLVLSTSGE
TARLVSKYRP KIPIITVTRN EQTARQIHLH RGCYPFWYPE PRGVQNHQWQ TDVDNRIRFG
LRNALALNVI QPGASIIAVQ GWKGGLGHTN TLRILTVPTD PADLELQPLG SL
