A0A2B7XAV5 · A0A2B7XAV5_POLH7

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

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, 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.

Type
IDPosition(s)Description
Binding site29ATP (UniProtKB | ChEBI)
Binding site92-93ATP (UniProtKB | ChEBI)
Binding site122-125ATP (UniProtKB | ChEBI)
Binding site123Mg2+ (UniProtKB | ChEBI); catalytic
Binding site168-170substrate; ligand shared between dimeric partners; in other chain
Active site170Proton acceptor
Binding site205substrate; ligand shared between dimeric partners
Binding site212-214substrate; ligand shared between dimeric partners; in other chain
Binding site268substrate; ligand shared between dimeric partners; in other chain
Binding site296substrate; ligand shared between dimeric partners
Binding site302-305substrate; ligand shared between dimeric partners; in other chain
Binding site485beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site542-546beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site580beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site587-589beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site647beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site673beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site679-682beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site754beta-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
      AJ80_08221

Organism names

  • Taxonomic identifier
  • Strain
    • UAMH7299
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenales incertae sedis > Polytolypa

Accessions

  • Primary accession
    A0A2B7XAV5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-394N-terminal catalytic PFK domain 1
Domain21-327Phosphofructokinase
Region395-408Interdomain linker
Domain409-704Phosphofructokinase
Region409-802C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    802
  • Mass (Da)
    87,719
  • Last updated
    2017-12-20 v1
  • Checksum
    320DC6A46A1BCF86
MATASSIPSTTLPIASSKRRRIAILTSGGDAPGMNGVVRAVIRMSIHCGSEAYAVHEGYEGLVQGGDLIKRMHWEDVRGWLSRGGTLIGSARSMSFMTREGRLKGAKNLVLRGIDALIVCGGDGSLTGADIFRAEWPGLLEELVQKKELTASDTDAYKHLNIVGVLGSIDNDMATTDATVGCYSSLTRICEAVDEVFDTAASHQRGFVVEVMGRHCGWLALMSAISTGADWLFIPEMPPRDGWEDDMCDIISNNRKRGKRRTIVIVAEGAQDKSLNRITSDAVKDILSNRLKLDTRVTVLGHTQRGGPACAYDRWLATLQGVEAVRAVLEATPASPSPIITIRENKIERASLVEAVRLTKSVATAINAQDFEKAISLRDAEFKAYHRAYINTATPHHRRLLIPENKRMRIAIIHVGAPAGGMNPATRAAVAYSRARGHTPVAIYNGFPGLCRHHADKPLGSVREVTWLEADAWVNEGGSEIGTNRGLPSEDMPQTANCFEIYKFDALFIIGGFEAFTAASQLRKAREQYPVFKIPIVVLPATISNNVPGTEYSLGSDTCLNALVNFCDVIRQSASSSRRRVFVIETQGGRSGYIATMAGLSIGAFAVYIPEEGIDIKTLARDIECLRHNFATDRGASHAGKIILRNETASSTYTTQFIADMIKEEARGRFESRAAVPGHFQQGGKPSPMDRIRAHRMAIKCIEHFESFWGVSPDDIAANPQSSAVIGVKGSEVIFSPMSGPEGLEETDTDWVYRRPKNEFWMSLHGLVDTLSGRTRDHQDGVFQMSEEEGWGKEMPRDTCHD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDNA01000181
EMBL· GenBank· DDBJ
PGH06115.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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