P21599 · KPYK2_ECOLI

Function

function

Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
K+ (UniProtKB | Rhea| CHEBI:29103 )

Activity regulation

Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site36substrate
Binding site38K+ (UniProtKB | ChEBI)
Binding site38-41ATP (UniProtKB | ChEBI)
Binding site40K+ (UniProtKB | ChEBI)
Binding site70K+ (UniProtKB | ChEBI)
Binding site77ATP (UniProtKB | ChEBI)
Binding site160ATP (UniProtKB | ChEBI)
Binding site223substrate
Site223Transition state stabilizer
Binding site225Mg2+ (UniProtKB | ChEBI)
Binding site251substrate
Binding site252Mg2+ (UniProtKB | ChEBI)
Binding site252substrate
Binding site284substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentpyruvate kinase complex
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionidentical protein binding
Molecular Functionkinase activity
Molecular Functionmagnesium ion binding
Molecular Functionpotassium ion binding
Molecular Functionpyruvate kinase activity
Biological Processglycolytic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate kinase II
  • EC number
  • Alternative names
    • PK-2

Gene names

    • Name
      pykA
    • Ordered locus names
      b1854, JW1843

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P21599

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001120732-480Pyruvate kinase II
Modified residue351N6-acetyllysine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homotetramer.

Binary interactions

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the pyruvate kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    480
  • Mass (Da)
    51,357
  • Last updated
    2007-01-23 v3
  • Checksum
    C37F004C374D27E9
MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE

Sequence caution

The sequence AAA96707.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict20in Ref. 7; AA sequence
Sequence conflict43in Ref. 7; AA sequence
Sequence conflict323in Ref. 6; AAA96707
Sequence conflict383in Ref. 6; AAA96707

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M63703
EMBL· GenBank· DDBJ
AAA24473.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC74924.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA15662.1
EMBL· GenBank· DDBJ
Genomic DNA
M77039
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
M87660
EMBL· GenBank· DDBJ
AAA96707.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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