U5H8Y7 · U5H8Y7_USTV1

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 site30ATP (UniProtKB | ChEBI)
Binding site158-159ATP (UniProtKB | ChEBI)
Binding site188-191ATP (UniProtKB | ChEBI)
Binding site189Mg2+ (UniProtKB | ChEBI); catalytic
Binding site234-236substrate; ligand shared between dimeric partners; in other chain
Active site236Proton acceptor
Binding site271substrate; ligand shared between dimeric partners
Binding site278-280substrate; ligand shared between dimeric partners; in other chain
Binding site335substrate; ligand shared between dimeric partners; in other chain
Binding site363substrate; ligand shared between dimeric partners
Binding site369-372substrate; ligand shared between dimeric partners; in other chain
Binding site544beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site601-605beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site639beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site646-648beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site706beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site732beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site811beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentmitochondrion
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
      MVLG_03682

Organism names

Accessions

  • Primary accession
    U5H8Y7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Region1-21Disordered
Region1-461N-terminal catalytic PFK domain 1
Domain22-69Phosphofructokinase
Domain134-395Phosphofructokinase
Domain475-764Phosphofructokinase
Region475-859C-terminal regulatory PFK domain 2
Region830-859Disordered
Compositional bias842-859Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    859
  • Mass (Da)
    92,793
  • Last updated
    2013-12-11 v1
  • Checksum
    0B3A5549B6BA73ED
MGYSPHPSMPSSPTGGQGRPTRLAVLTSGGDCSGMNAAVRAVVKMGISRGCEVYVVREGWEGLVRGNENEEPTTSQLTTSNLIPFNSTNAAAASANARPTERKPSRERGGFVATYGEGELLKEGEGEQTLRNRFILRVGWDDVRGFASLGGTLIGTARCAAFRELEGRRKAAFNLVKHGIDALVVCGGDGSLTGADRLRAEWPDHVQALLKSGQITPEQFEAHQHLNIVGLVGSIDNDMAGTDMTIGATTALHRICEAVDSISSTASSHSRAFVVEVMGRNCGWLALMAAIATGADYMFIPERPPTAEDWQTSMCTVLGRHRAEGKRKTIIIVAEGAHDCNLKPISPEEIKDVLTQRLGLDTRVTTLGHTQRGGAPAAYDRILATLQGAEAVEAVLASTVDSPSPVIGIQENKIQRQPLMEAVKKTQDVAKAIADKDFARALSLRDPEFEDCLHAFRATTRLNETCRVPEKQKMRIAIIHTGAPAGGMNAATRTAVRYCLCHGHTPLAIYNGFVGLLHGNVAELSWLRVDQWSTRGGSELGTNRVLPDTDLAGVAAKLAEYKIDGLLIVGGFEAMVSLEQLEKGRKDHAALRIPLIHLPATISNNVPITEWSVGSDTSINVLVEACDSIKQSASASRNRVFVVETQGAGCGYIAMLGALATGANLVYTPENGISLGMLQRDVEFLKKRYSQDVAGKSEGRLIILSEKASKTYTTQVVTNIFAEEGKDSFDARSVALGHTLQGGVPSPRDRTRAIRLTVKCIDFLEKHHNQKLQNLAPDPQDPDAATIVIEGASIRFASLEEMVQAADFKNRRGKVQWWTSAKELVETMAGKKVPSEELKTPLTSPRTEKKDPNERFSRL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Compositional bias842-859Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEIJ01000359
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
GL541678
EMBL· GenBank· DDBJ
KDE06000.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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