ID   KPYK_MYCIT              Reviewed;         472 AA.
AC   P94939;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 106.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; Synonyms=pykF;
OS   Mycobacterium intracellulare.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Batty;
RA   Alavi M.R., Rouse D.A., Morris S.L.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+);
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;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
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; U65430; AAB39214.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94939; -.
DR   SMR; P94939; -.
DR   OMA; AAALXEI; -.
DR   UniPathway; UPA00109; UER00188.
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   FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1.
DR   FunFam; 3.40.1380.20:FF:000009; Pyruvate kinase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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   NCBIfam; NF004491; PRK05826.1; 1.
DR   NCBIfam; NF004886; PRK06247.1; 1.
DR   NCBIfam; NF004978; PRK06354.1; 1.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT   CHAIN           1..472
FT                   /note="Pyruvate kinase"
FT                   /id="PRO_0000112080"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         35
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
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         74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            218
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   472 AA;  50462 MW;  A9D58F3E64E117D1 CRC64;
     MSRRGKIVCT LGPATNSDEL ILALVEAGMD VARLNFSHGD YADHKAAYER VRVASDATGR
     AVGVLADLQG PKIRLGRFAT GPTYWADGET VRITVADCEG SHDRVSTTYK KLAEDAAVGD
     RVLVDDGKVC LVVDGIEGDD VICTVVEGGP VSNNKGISLP GMNVSAPALS EKDIEDLTFA
     LDLGVDLVAL SFVRSPADVE LVHEVMDRVG RRVPVIAKLE KPEAVDNLET IVLAFDAIMV
     ARGDLGVELP LEEVPLVQKR AIQMARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV
     LDGADAVMLS GETSVGKYPM AAVRTMSRII CAVEDNSTAA PPLTHVPRTK RGVISYAARD
     IGERLDAKAL VAFTQSGDTV KRLARLHTPL PLLAFTAWPE VRSQLAMTWG TETFIVPMMT
     STGGMIRQVD KSLLELGRYK RGDLVVIVAG APPGTVGSTN LIHVHRIGED DV
//