A0A3B3IMJ2 · A0A3B3IMJ2_ORYLA

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.

Type
IDPosition(s)Description
Binding site33ATP (UniProtKB | ChEBI)
Binding site96-97ATP (UniProtKB | ChEBI)
Binding site126-129ATP (UniProtKB | ChEBI)
Binding site127Mg2+ (UniProtKB | ChEBI); catalytic
Binding site172-174substrate; ligand shared between dimeric partners; in other chain
Active site174Proton acceptor
Binding site209substrate; ligand shared between dimeric partners
Binding site216-218substrate; ligand shared between dimeric partners; in other chain
Binding site272substrate; ligand shared between dimeric partners; in other chain
Binding site332substrate; ligand shared between dimeric partners
Binding site338-341substrate; ligand shared between dimeric partners; in other chain
Binding site512beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site620-624beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site658beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site665-667beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site721beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site747beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site753-756beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site827beta-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
      PFKP

Organism names

  • Taxonomic identifier
  • Strain
    • Hd-rR
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Atherinomorphae > Beloniformes > Adrianichthyidae > Oryziinae > Oryzias

Accessions

  • Primary accession
    A0A3B3IMJ2

Proteomes

Subcellular Location

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-430N-terminal catalytic PFK domain 1
Domain26-286Phosphofructokinase
Domain287-363Phosphofructokinase
Region443-874C-terminal regulatory PFK domain 2
Domain596-779Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    874
  • Mass (Da)
    95,502
  • Last updated
    2018-12-05 v1
  • Checksum
    2636B346A5AB08F1
MAGNAGPKRQDTRKFVENLSGEGKCIAVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIHEGYQGMVDGGDNIKEATWESVSSMLQVGGTVIGSARCKEFRTHEGRLKAAHNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLNELLEQGLINEEAVSSNSVLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFIPEMPPDDGWEDNMCQKLSESRSRGSRLNIIIVAEGATDRQGQHITSSFVKDNRADKKRLNIIIVAEGAIDSHNKAITPDCIKDLVVRCLGFDTRVTILGHVQRGGTPSAFDRILGSRMGVEAVLALLEASTDTPACVVSLVGNQAVRLPLMECVQMTQEVQKAMDEKKFDEAVRLRGRSFENNLSTYRLLSYRKLDSELPNSSFNVAVLNVGAPAAGMNAAVRSAVRVGITEGHKMFAVNDGFEGFAKGQIKEIKWGDVGGWTGQGGSLLGTKRTLPAKRLAKIAEQMRIHNINALLVIGGFEAYVGLLELSSARDEYPEFCVPMVMVPATVSNNIPGSDLSIGSDTALNAITDAFESLLELYEARAHHEEFCIPMCILPATISNNVPGTDHSLGADTSLNAIVETCDRIKQSASGTKRRVFIIETMGGYCGYLATVGGLAAGADTVYIYEEAFDIRDLQANVEHLTQKMKTTIQRGLVLRNENCNENFTTDFIYQLYSEEGRGVFDCRKNILGHMQQGGAPSPFDRNFGTKVAAKAMQWITRALKESYKGGKVFTNAEDTACLLGMRRRAMVFQPVAQLREETDFEHRIPKDQWWLKLRPLMKILAKYKTSYDVSDAGQLEHVTRVRPKDFQPSV

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3B3HD46A0A3B3HD46_ORYLAPFKP842
A0A3B3IGG9A0A3B3IGG9_ORYLAPFKP842
A0A3B3HFI8A0A3B3HFI8_ORYLAPFKP736
A0A3B3IIB5A0A3B3IIB5_ORYLAPFKP823
A0A3B3IIQ0A0A3B3IIQ0_ORYLAPFKP823
H2LMF2H2LMF2_ORYLAPFKP756
A0A3B3HTR3A0A3B3HTR3_ORYLAPFKP759
A0A3B3H5T7A0A3B3H5T7_ORYLAPFKP740

Keywords

Genome annotation databases

Similar Proteins

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