C0E6V7 · C0E6V7_9CORY

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site10ATP (UniProtKB | ChEBI)
Binding site72-73ATP (UniProtKB | ChEBI)
Binding site102-105ATP (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI); catalytic
Site104Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site125-127substrate; ligand shared between dimeric partners; in other chain
Active site127Proton acceptor
Binding site162substrate; ligand shared between dimeric partners
Binding site169-171substrate; ligand shared between dimeric partners; in other chain
Binding site222substrate; ligand shared between dimeric partners; in other chain
Binding site266substrate; ligand shared between dimeric partners
Binding site272-275substrate; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Molecular Function6-phosphofructokinase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
Molecular Functionfructose-6-phosphate binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionmonosaccharide binding
Biological Processcanonical glycolysis
Biological Processfructose 1,6-bisphosphate metabolic process
Biological Processfructose 6-phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent 6-phosphofructokinase
  • EC number
  • Short names
    ATP-PFK
    ; Phosphofructokinase
  • Alternative names
    • Phosphohexokinase

Gene names

    • Name
      pfkA
    • ORF names
      CORMATOL_02745

Organism names

Accessions

  • Primary accession
    C0E6V7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-297Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    37,082
  • Last updated
    2009-05-05 v1
  • Checksum
    5AD986B5AA2DE48B
MRIATLTSGGDCPGLNAVIRGIVRTATEYGSTVVGYEDGWVGLMEDRRIQLYDDENIDRILLRGGTILGTGRLHPDKFKSGLEQIRENLEEAGIDALIPIGGEGTLKGAKWLSDNGIPVVGVPKTIDNDVNGTDYTFGFDTAVSVATDAIDRLHTTAESHNRVMIVEVMGRHVGWIALHAGMAGGAHYIVIPEVPFDIAEITKAMERRFQLGEKYGIIVVAEGALPKPGTMDFTEGAVDQFGHQVFNGIGQVIGDEIKKRLGHDVRTTTLGHIQRGGTPTAFDRVLATRYGVHATRACHDKDFGKCVALRGEHVELIDLEDAVGKLKVVPDSRYRTARALFG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACEB01000046
EMBL· GenBank· DDBJ
EEG25817.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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