A0A2A4IL26 · A0A2A4IL26_9SPIR

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    pfkA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 )

Activity regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.

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 site14ATP (UniProtKB | ChEBI)
Binding site24-28ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site75-76ATP (UniProtKB | ChEBI)
Binding site105-108ATP (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI); catalytic
Binding site130-132substrate; ligand shared between dimeric partners; in other chain
Active site132Proton acceptor
Binding site159ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site167substrate; ligand shared between dimeric partners
Binding site174-176substrate; ligand shared between dimeric partners; in other chain
Binding site190-192ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site216ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site218-220ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site227substrate; ligand shared between dimeric partners; in other chain
Binding site250substrate; ligand shared between dimeric partners
Binding site256-259substrate; 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
      pfkA
    • ORF names
      KQ44_14285

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • G79
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Brachyspirales > Brachyspiraceae > Brachyspira

Accessions

  • Primary accession
    A0A2A4IL26

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-282Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    326
  • Mass (Da)
    34,854
  • Last updated
    2017-12-20 v1
  • MD5 Checksum
    56561C0811369BF6E8E9A37092D878F2
MSDIKKIGVLTSGGDASGMNPAIRSVVRTAIANGLEVMGIKEGYQGLMYNDVYPMTAGSVGGIINHGGTILFSARSPEFQTEDGMKKAADNMRYHGMDALIVIGGDGTYKGALDFYNHHPDFPIVAIPGTIDNDIFGTDYTIGYDTAVNVAMDAIDKLRDTATSHGRCFVVEVMGRHAGYIALEVGIASGAEDILIPETTTDMDKIVEELQIAKKRGKKSSIIVVAEGDESGGAMEVAKQIEGKTGFDTRVTILGHMQRGGSPTSRERLMAARFGYIAVKALLEGKKNVAVGIWKGEYTYTPLTDAVKKVPKVDPIDLALCRTLAI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQIU01000009
EMBL· GenBank· DDBJ
PCG18868.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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