A0A8M9PRJ5 · A0A8M9PRJ5_DANRE

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 site25ATP (UniProtKB | ChEBI)
Binding site88-89ATP (UniProtKB | ChEBI)
Binding site118-121ATP (UniProtKB | ChEBI)
Binding site119Mg2+ (UniProtKB | ChEBI); catalytic
Binding site164-166substrate; ligand shared between dimeric partners; in other chain
Active site166Proton acceptor
Binding site201substrate; ligand shared between dimeric partners
Binding site208-210substrate; ligand shared between dimeric partners; in other chain
Binding site264substrate; ligand shared between dimeric partners; in other chain
Binding site292substrate; ligand shared between dimeric partners
Binding site298-301substrate; ligand shared between dimeric partners; in other chain
Binding site477beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site534-538beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site572beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site579-581beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site635beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site661beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site667-670beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site741beta-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 Componentmembrane
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
      pfkpb

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    A0A8M9PRJ5

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-390N-terminal catalytic PFK domain 1
Domain18-323Phosphofructokinase
Domain408-693Phosphofructokinase
Region408-787C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    787
  • Mass (Da)
    86,034
  • Last updated
    2022-08-03 v1
  • Checksum
    65D6298AEAD98FE0
MPDTKKYIENLSGAGKCIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIHEGYQGMVDGGDNIKEASWESVSSMLQVGGTVIGSARCKDFRTHEGRLCAALNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQSGQISEDAAQTHSALHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVLIPERPPKDGWEEQMCQKLSENRADKKRLNIIIVAEGAIDQNNKPITTDHIKDLVVSRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLEASPGTPACVVSLCGNQAVRVPLMECVQMTQEVQKAMDEKRFEEAVKLRGRSFENNLNTYKLLSHRKIDTELPHDGQCRSSFNVAVLNVGAPAAGMNAAVRSAVRVGITEGHTMFAVSDGFEGFYKGQIKEIKWGDVGGWTGQGGSLLGTKRTLPAKHVDKIAEQMRIHNINALLVIGGFEAYLGLMELQAARSKHAELCVPMVMVPATVSNNIPGSDLSIGADTAINAITDTCDRIKQSASGTKRRVFIIETMGGYCGYLATVGGLAAGADAAYIYEEPFDIRDLQSNVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKIAAKAMQWISKKLKEFYRDGRVFANTEDSACLLGMRRRALLFQPVVQLKDETDFVHRIPKEQWWLRLRPLMKILAKYKTSYDVSDSGQLEHIVRLRAKDSSAI

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8M9PAY2A0A8M9PAY2_DANREpfkpb789
A0A8M9PJ31A0A8M9PJ31_DANREpfkpb784
X1WDM7X1WDM7_DANREpfkpb782
A0A8M9PQ30A0A8M9PQ30_DANREpfkpb784
A0A8M9PNB0A0A8M9PNB0_DANREpfkpb787
A0A8M9P1U9A0A8M9P1U9_DANREpfkpb782
A0A8M9PAZ4A0A8M9PAZ4_DANREpfkpb738
A0A8M2BAP4A0A8M2BAP4_DANREpfkpb782
A0A8M9PGE2A0A8M9PGE2_DANREpfkpb789
A0A8M9PGF5A0A8M9PGF5_DANREpfkpb782
A0A8M6YU07A0A8M6YU07_DANREpfkpb731

Keywords

Sequence databases

Similar Proteins

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