KPYK_STAHJ
ID KPYK_STAHJ Reviewed; 586 AA.
AC Q4L739;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=SH1227;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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 -!- 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; AP006716; BAE04536.1; -; Genomic_DNA.
DR RefSeq; WP_011275526.1; NC_007168.1.
DR AlphaFoldDB; Q4L739; -.
DR SMR; Q4L739; -.
DR STRING; 279808.SH1227; -.
DR EnsemblBacteria; BAE04536; BAE04536; SH1227.
DR GeneID; 58062574; -.
DR KEGG; sha:SH1227; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 1098983at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000543; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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; SSF52009; SSF52009; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..586
FT /note="Pyruvate kinase"
FT /id="PRO_0000294139"
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 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 222
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 246
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 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 586 AA; 63019 MW; E6C0B61B47DCE8CE CRC64;
MRKTKIVCTI GPASESEEML EKLMKAGMNV ARLNFSHGSH EEHKARIDTI RKVADRLGKT
IGILLDTKGP EIRTHDMKDG LIMLEKGKEV IVSMSQVEGT PEKFSVTYED LINDVQVGSY
ILLDDGLVEL QVKDIDKTKG EVKCDILNTG ELKNKKGVNL PGVKVNLPGI TDKDADDILF
GIKEDVDYIA ASFVRRPSDV LDIREILERE NNHNITIFPK IENQEGIDNI EEILEVSDGL
MVARGDMGVE IPPESVPIVQ KDLIRKCNKL GKPVITATQM LDSMQRNPRA TRAEASDVAN
AIYDGTDAVM LSGETAAGLY PEEAVKTMRN IAVSAEAAQD YKKLLSDRTK LVETSLVNAI
GVSVAHTALN LNVKAIVAAT ESGSTAVTIS KYRPHSDIIA VTPSEHTARQ LALVWGAYPV
IKKGRKTTDD LLNNAVATAV ETGRVTNGDL IIITAGVPTG EKGTTNMMKL HLVGDEIAKG
QGVGRGSVVG KTVVANSASD LEGVDLSESV IVTNSVDETL VPYIEQAVGL ITEENGITSP
SAIIGLEKSI PTIIGVENAT KELKDGILVT VDAAQGKIFE GYANVL
