KPYK_CLOPE
ID KPYK_CLOPE Reviewed; 474 AA.
AC Q46289;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pykF; OrderedLocusNames=CPE2149;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=CPN50;
RX PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995;
RA Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT "Rapid expansion of the physical and genetic map of the chromosome of
RT Clostridium perfringens CPN50.";
RL J. Bacteriol. 177:5680-5685(1995).
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; BA000016; BAB81855.1; -; Genomic_DNA.
DR EMBL; X86495; CAA60217.1; -; Genomic_DNA.
DR RefSeq; WP_011010789.1; NC_003366.1.
DR AlphaFoldDB; Q46289; -.
DR SMR; Q46289; -.
DR STRING; 195102.gene:10491419; -.
DR EnsemblBacteria; BAB81855; BAB81855; BAB81855.
DR KEGG; cpe:CPE2149; -.
DR HOGENOM; CLU_015439_9_0_9; -.
DR OMA; FERCDES; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000818; Chromosome.
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 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..474
FT /note="Pyruvate kinase"
FT /id="PRO_0000112066"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 34..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 34
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 73
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 221
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 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="E -> G (in Ref. 2; CAA60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> G (in Ref. 2; CAA60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="E -> G (in Ref. 2; CAA60217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52082 MW; 387970D750B2B39B CRC64;
MQKTKMIFTI GPSSDSEEIL REFIRIGMNA ARLNFSHGDH ASHKEKIELI KRLRKEEKSA
TAILLDIKGP KIRTYNFKNG EAELKNGDEF TFSCGDEILG DNTKCSISYK ELYEDIKPGG
SILVDDGLLE FKVKEVRGTD IICEVIEGGT IKDHKGVNVP NVPIKLPAVT EKDRSDLIFG
CEMEVDFVAA SFIRKPEDVL EVREILDSHG GKDIKIISKI ESQEGVDNIK EIIKVTDGVM
VARGDMGVEI PIENVPIIQK NIIKKCNQAG KIVITATQML DSMIRNPRPT RAEASDVCNA
IFDGTDAIML SGESASGSFP IEAAMTMSRI AKKAEANLDY NYLLRRLKDP NPNPDAFADA
ISYSASKTAS KFPTKAIVAA TQTGSTAKIL SKYKPSCPII AITPYEKVRR SLALNFGIIS
KKCAYFNSTD EIIEEARKVA KEFEIAETGD NIMVAAGFPT SITGGTNMLK IEKI
