T1FP07 · T1FP07_HELRO

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 site44ATP (UniProtKB | ChEBI)
Binding site107-108ATP (UniProtKB | ChEBI)
Binding site137-140ATP (UniProtKB | ChEBI)
Binding site138Mg2+ (UniProtKB | ChEBI); catalytic
Binding site183-185substrate; ligand shared between dimeric partners; in other chain
Active site185Proton acceptor
Binding site220substrate; ligand shared between dimeric partners
Binding site227-229substrate; ligand shared between dimeric partners; in other chain
Binding site283substrate; ligand shared between dimeric partners; in other chain
Binding site311substrate; ligand shared between dimeric partners
Binding site317-320substrate; ligand shared between dimeric partners; in other chain
Binding site491beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site549-553beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site587beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site594-596beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site650beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site676beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site682-685beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site757beta-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

    • Name
      20210554
    • ORF names
      HELRODRAFT_186529

Organism names

Accessions

  • Primary accession
    T1FP07

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-409N-terminal catalytic PFK domain 1
Domain37-342Phosphofructokinase
Region422-799C-terminal regulatory PFK domain 2
Domain423-708Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    799
  • Mass (Da)
    87,224
  • Last updated
    2013-10-16 v1
  • Checksum
    00EB1757B6F66F7B
MDDSAALGKIQKSQSICVTAGTEGKKIEKDCYSGCVIGVFTSGGDSQGMNAATRAIVRMGIYVGCKVYLIKEGYQGMVDGGSNIVLADWKSVSNIIQSGGTIIGSARCADFRERPGRLQAAYNLLERGITNLVCIGGDGSLTGANLFRIEWSSLLEELVKTGRITSQKAQECAHLNVVGLVGSIDNDFCGTDMTIGTDSALHRIIEAIDNINTTASSHQRCFVMEVMGRHCGYLALVAALASEADWVFIPESPPEKGWEDKLCEKLAQERSLGQRLNIIIVSEGAIDEEGRPITADQIKDLISKRLKYDTRVTILGHVQRGGNPSAFDRLLGCRMGAEAVLALMEATPFTPACVISLNGNQIVRVPLMECVARTKEVQAAMDKKEFQKAVELRGRDFVANLESFRTLARARAPKKAFCTAFNLAVVFVGAPACGMNAAVRSFVRIGITKGFRILGIKNGFEGLVNNEVVSLSWTDVHGWSGSGGARLKTNRTTPSKVGLDRVADKLRHFSIHGLLIIGGFEAFESILQLTEARSAYREFCIPMSMVPATISNNIPGTDFSLGSDTSLNAIVEIADRIKQSASGTRNRVFVLETMGGHCGYLATLSALASGADAAYIFEEPFNITDLQGDVNHLASKIRGGVKRGMVMRNEKANENYTSDFITRLYQEEGRNIFQCRLNVLGHMQQGGQPSPFDRNMGTKMAAKCAELLAKQVEENKTPEGSVFTNSSDTATLLGLQKKRSLFTPVLELKEKTDFQHRISKEVWWCKLRPLLRILAMHNSIYEVEGQENDGFDDLDKLYL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMQM01001367
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KB097495
EMBL· GenBank· DDBJ
ESN96243.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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