A0A0N4TMH1 · A0A0N4TMH1_BRUPA

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.

TypeIDPosition(s)Description
Binding site62ATP (UniProtKB | ChEBI)
Binding site125-126ATP (UniProtKB | ChEBI)
Binding site155-158ATP (UniProtKB | ChEBI)
Binding site156Mg2+ (UniProtKB | ChEBI); catalytic
Binding site201-203substrate; ligand shared between dimeric partners; in other chain
Active site203Proton acceptor
Binding site238substrate; ligand shared between dimeric partners
Binding site245-247substrate; ligand shared between dimeric partners; in other chain
Binding site301substrate; ligand shared between dimeric partners; in other chain
Binding site329substrate; ligand shared between dimeric partners
Binding site335-338substrate; ligand shared between dimeric partners; in other chain
Binding site508beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site565-569beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site603beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site610-612beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site692beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site698-701beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site774beta-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
      BPAG_LOCUS9605

Organism names

Accessions

  • Primary accession
    A0A0N4TMH1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-427N-terminal catalytic PFK domain 1
Domain55-360Phosphofructokinase
Domain441-724Phosphofructokinase
Region441-813C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    813
  • Mass (Da)
    89,500
  • Last updated
    2015-12-09 v1
  • Checksum
    71CBBC91579D7CC8
MKNSGLPITSLDDDFGPPTTDMHRMKFSIRSDSIVPSAGREGTSIAPQIYKGRTMAVFTSGGDASGMNSAVRSVVRMGVYLGCRVFLIYEGYQGMVDGGDNIKEADWQSVSDIIQRGGTVIGSARCKVFQERWGRLQAAENLIKHRITNLVCIGGDGSLTGANLFRQEWQGLVKELLLSGKITREEAVECGNIQIVGLVGSIDNDFCGTDMTIGTDTALQRICEAIDCVMSTAQSHQRTFVIEVMGRHCGYLALVAALASEADFCFIPEWPVPTDWPTVLCQKLRMMREAGSRLNIVIVAEGALDREGKCITAESVRAVVKETLHYDTRVTVLGHVQRGGSPSAFDRLLGCRMGAEAVLALMEMTPQSEPCVVSIDGNVIVRVPLMQCVQRTQAVKKAMDERDWETAVKLRGRSFQRNLETYRLLTKVEPKKVDPNVPVYNVAIVNVGAPAGGMNAVVRSYVRMALYHGCKVYGIKNSFEGLCRGEDMAWGDVCNWVMYGGSFLGTQKQLPGKIMDKVADAFEKYNFHGLLLVGGFEAFHSCLLLSRARDKYPSLRIPMCVIPCTISNNVPGTSLSLGSDTAVNEICEMIDKIKLSATGTKRRVFIVETMGGFCGYLATISALASGADNAYIFEEQFKVSDIMDDVKVISRKMRTGVQRYLIVRNECANKNYTTEFVNQLFAEEGKGAFSTRTNVLGHAQQGGNPTPFDRNMGTKLAARALEFIISQILKYIDPKTGILNAVSPDSATLLGLMGRRTVFTPVEELSLETDFEHRVPKHQWWMKMRPLLRILAKHDSTYQTEAMVVPEVEGESA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UZAD01013160
EMBL· GenBank· DDBJ
VDN90791.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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