A0A085BGF1 · A0A085BGF1_9FLAO

  • 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 site16ATP (UniProtKB | ChEBI)
Binding site26-30ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site77-78ATP (UniProtKB | ChEBI)
Binding site107-110ATP (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI); catalytic
Binding site131-133substrate; ligand shared between dimeric partners; in other chain
Active site133Proton acceptor
Binding site160ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site168substrate; ligand shared between dimeric partners
Binding site175-177substrate; ligand shared between dimeric partners; in other chain
Binding site219-221ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site228substrate; ligand shared between dimeric partners; in other chain
Binding site252substrate; ligand shared between dimeric partners
Binding site258-261substrate; 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
      IO90_06145

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FH1
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium

Accessions

  • Primary accession
    A0A085BGF1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-281Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    328
  • Mass (Da)
    35,178
  • Last updated
    2014-10-29 v1
  • Checksum
    7E7DFD2221C8A412
MSENNIKSIAVLTSGGDAPGMNAALRAVVRTANHFNIDCYGIREGYNGLIAGDVTKMGPRSVKNIINQGGTILKSARSKEFMTPEGRKKAFEQCQKLGIDALVCIGGDGSFTGAKVFNEEFGIKVIGVPGTIDNDIFGTDKTIGYDTALNTAMDAIDKIRDTATSHNRVFFVEVMGRDAGFIALNSGIATGALDILIPERKDSLEDLFSTFRTAEKVGKSSSIVVVAEGEELASIYDLAKATKEEFPSYDIRVTILGHIQRGGSPSCADRVLASNLGYGAVIGLMEGKNKVMVGMQSNKIVYTPIEEAIKKHNEIDKDLLKIAEILAM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPLZ01000005
EMBL· GenBank· DDBJ
KFC21546.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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