A0A158QAU1 · A0A158QAU1_ENTVE

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

Pathway

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

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site61ATP (UniProtKB | ChEBI)
Binding site124-125ATP (UniProtKB | ChEBI)
Binding site154-157ATP (UniProtKB | ChEBI)
Binding site155Mg2+ (UniProtKB | ChEBI); catalytic
Binding site200-202substrate; ligand shared between dimeric partners; in other chain
Active site202Proton acceptor
Binding site237substrate; ligand shared between dimeric partners
Binding site244-246substrate; ligand shared between dimeric partners; in other chain
Binding site300substrate; ligand shared between dimeric partners; in other chain
Binding site328substrate; ligand shared between dimeric partners
Binding site334-337substrate; ligand shared between dimeric partners; in other chain
Binding site511beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site568-572beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site606beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site613-615beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site669beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site695beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site701-704beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site777beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; 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 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

    • ORF names
      EVEC_LOCUS6407

Organism names

Accessions

  • Primary accession
    A0A158QAU1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-426N-terminal catalytic PFK domain 1
Domain54-359Phosphofructokinase
Domain443-725Phosphofructokinase
Region443-819C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    819
  • Mass (Da)
    89,964
  • Last updated
    2016-06-08 v1
  • Checksum
    6BF5C6EFE75579E3
MGDVPESGSPTEDPSPLTTFLRQRFSSGRSDSIIPTEGREGTKITRLQYSGKVMAVFTSGGDAPGMNSAVRSVVRMGIYLGCTVYFINEGYQGMVDGGDNIRKADWNSVSDIIQKGGTIIGSARCKDFREHSGRLKAAENLIAHGITNLVCIGGDGSLTGANLFRQEFPTLVQELLNAGRITKEQAEQCSNIQIVGMVGSIDNDFCGTDMTIGTDTALQRIIEAVDSVMSTAQSHQRSFVIEVMGRHCGYLALIAALASEADFCFIPEWPVPVDWPKVLCEKLQVMRNQGQRLNIIIVAEGAIDRDGKAITAELVRSVIKSTLHYDTRVTVLGHVQRGGMPSAFDRLLGCRMGAEAVLALMEMTPASQPCVISIDGNLMCRVPLMESVKRTQAVQKAMDEHQWQEAVKLRGHSFQRNLDTYRLLAKLRIPKEKDNLSEGMKFNVAVMNVGAPAGGMNAAVRSFVRMGIYHRCKVYGINNSFEGLAAGNLKMQWSDVTNWVMHGGSFLGTQKQLPESKMPQIANSLEKFNIHALLIIGGFEAYNACLMLYRAREQYKALRIPMVVIPATISNNLPGTSISLGSDTALNEICRMIDKIKQSATGTKRRVFIVETMGGFCGYLATLAALASGADNAYIFEEPFNVNDILEDVKVITEKMKKGVQRYLIIRCELANRNYTTEFVKQVFSEEGKGSFSTRTNVLGHAQQGGSPTPFDRNLGTKLAAVALEQLIKQAKETFDKATETVNAIEPETATLLGLQGREVVFTAVEKLATETDFEHRLPKEQWWLRVRPLLRILAQHEELAIQAEAELALRADTKGIIG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UXUI01008498
EMBL· GenBank· DDBJ
VDD91656.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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