A0A154BV93 · A0A154BV93_ANASB

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 site14ATP (UniProtKB | ChEBI)
Binding site76-77ATP (UniProtKB | ChEBI)
Binding site116-119ATP (UniProtKB | ChEBI)
Binding site117Mg2+ (UniProtKB | ChEBI); catalytic
Site118Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site139-141substrate; ligand shared between dimeric partners; in other chain
Active site141Proton acceptor
Binding site176substrate; ligand shared between dimeric partners
Binding site183-185substrate; ligand shared between dimeric partners; in other chain
Binding site236substrate; ligand shared between dimeric partners; in other chain
Binding site280substrate; ligand shared between dimeric partners
Binding site286-289substrate; 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
      AXX12_16665

Organism names

  • Taxonomic identifier
  • Strain
    • RU4
  • Taxonomic lineage
    Bacteria > Bacillota > Negativicutes > Selenomonadales > Sporomusaceae > Anaerosporomusa

Accessions

  • Primary accession
    A0A154BV93

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-312Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    362
  • Mass (Da)
    38,534
  • Last updated
    2016-06-08 v1
  • Checksum
    AB7927E39738CFF1
MTTVKTIGILTGGGDCPGLNAVIRAAVKTALRRGIRVWGVQNGFGGLVEDQMVELDDRSVSGILPRGGTILGTTNRDNPFAYAVEIDGKTQYQDMSAKALENLRSKGIEALIVIGGDGSLAIAAKFNALGLPVVGVPKTIDNDIPGTERTFGFDTAVSIAGEALDRLHTTAESHHRVMVLEVMGRYAGWIALHAGLAGGADCILIPEIPYRMESVLEKISRRRQVGKHFSLIVIAEGAKPENGEVTISRIVENSHEKIRLGGVGEKLAREVESSTGLESRCTVLGHVQRGGTPTAFDRVLCTRYGVAAAECLVEGVSGCMVALRQDRIIRLPIVDIAGRSRQIEPDDELVCAGRAIGICFGD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LSGP01000005
EMBL· GenBank· DDBJ
KYZ77896.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp