KPYK_LACDE
ID KPYK_LACDE Reviewed; 589 AA.
AC P34038;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk;
OS Lactobacillus delbrueckii subsp. bulgaricus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8755908; DOI=10.1128/jb.178.15.4727-4730.1996;
RA Branny P., de la Torre F., Garel J.R.;
RT "The genes for phosphofructokinase and pyruvate kinase of Lactobacillus
RT delbrueckii subsp. bulgaricus constitute an operon.";
RL J. Bacteriol. 178:4727-4730(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RX PubMed=8366023; DOI=10.1128/jb.175.17.5344-5349.1993;
RA Branny P., de la Torre F., Garel J.R.;
RT "Cloning, sequencing, and expression in Escherichia coli of the gene coding
RT for phosphofructokinase in Lactobacillus bulgaricus.";
RL J. Bacteriol. 175:5344-5349(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1-40, AND CHARACTERIZATION.
RX PubMed=8274531; DOI=10.1016/0300-9084(93)90130-k;
RA le Bras G., Garel J.R.;
RT "Pyruvate kinase from Lactobacillus bulgaricus: possible regulation by
RT competition between strong and weak effectors.";
RL Biochimie 75:797-802(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;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- ACTIVITY REGULATION: Strongly activated by glucose-6-phosphate, ribose-
CC 5-phosphate and fructose-6-phosphate. Weak activator AMP and weak
CC inhibitor fructose-1,6-bisphosphate can act as strong inhibitors in the
CC presence of strong activators.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; X71403; CAA50527.1; -; Genomic_DNA.
DR PIR; B48663; B48663.
DR PIR; S35929; S35929.
DR RefSeq; WP_003619815.1; NZ_QOVB01000006.1.
DR AlphaFoldDB; P34038; -.
DR SMR; P34038; -.
DR GeneID; 66399782; -.
DR OMA; QVPIVQK; -.
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; IPR008279; PEP-util_enz_mobile_dom.
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; PF00391; PEP-utilizers; 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 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Direct protein sequencing; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate;
KW Transferase.
FT CHAIN 1..589
FT /note="Pyruvate kinase"
FT /id="PRO_0000112076"
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 67
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 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 221
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 589 AA; 62920 MW; 2BA3D3CF7AE290F1 CRC64;
MKKTKIVSTL GPASDDIETI TKLAEAGANV FRFNFSHGNH EEHLARMNMV REVEKKTGKL
LGIALDTKGA EIRTTDQEGG KFTINTGDEI RVSMDATKAG NKDMIHVTYP GLFDDTHVGG
TVLIDDGAVG LTIKAKDEEK RELVCEAQNT GVIGSKKGVN APGVEIRLPG ITEKDTDDIR
FGLKHGINFI FASFVRKAQD VLDIRALCEE ANASYVKIFP KIESQEGIDN IDEILQVSDG
LMVARGDMGV EIPFINVPFV QKTLIKKCNA LGKPVITATQ MLDSMQENPR PTRAEVTDVA
NAVLDGTDAT MLSGESANGL YPVQSVQAMH DIDVRTEKEL DTRNTLALQR FEEYKGSNVT
EAIGESVVRT AQELGVKTII AATSSGYTAR MISKYRPDAT IVALTFDEKI QHSLGIVWGV
EPVLAKKPSN TDEMFEEAAR VAKEHGFVKD GDLVIIVAGV PFGQSGTTNL MKLQIIGNQL
AQGLGVGTGS VIGKAVVANS AEEANAKVHE GDILVAKTTD KDYMPAIKKA SGMIVEASGL
TSHAAVVGVS LGIPVVVGVA DATSKIADGS TLTVDARRGA IYQGEVSNL
