A0A7I2V3Z0 · A0A7I2V3Z0_HUMAN

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    PFKP
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

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.

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 site59-60ATP (UniProtKB | ChEBI)
Binding site89-92ATP (UniProtKB | ChEBI)
Binding site90Mg2+ (UniProtKB | ChEBI); catalytic
Binding site135-137substrate; ligand shared between dimeric partners; in other chain
Active site137Proton acceptor
Binding site172substrate; ligand shared between dimeric partners
Binding site179-181substrate; ligand shared between dimeric partners; in other chain
Binding site235substrate; ligand shared between dimeric partners; in other chain
Binding site263substrate; ligand shared between dimeric partners
Binding site269-272substrate; ligand shared between dimeric partners; in other chain
Binding site443beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site500-504beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site538beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site545-547beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site601beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site627beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site633-636beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site706beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
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
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A0A7I2V3Z0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,076 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)275PRIDEPhosphothreonine
Modified residue (large scale data)348PRIDEPhosphoserine
Modified residue (large scale data)613PRIDEPhosphotyrosine
Modified residue (large scale data)745PRIDEPhosphoserine

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-294Phosphofructokinase
Region1-361N-terminal catalytic PFK domain 1
Domain374-659Phosphofructokinase
Region374-746C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    746
  • Mass (Da)
    81,800
  • Last updated
    2021-04-07 v1
  • Checksum
    DEA251EF304F0133
MNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQPWSV

Computationally mapped potential isoform sequences

There are 10 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q01813PFKAP_HUMANPFKP784
H0Y757H0Y757_HUMANPFKP103
H0Y3Y3H0Y3Y3_HUMANPFKP166
V9GY25V9GY25_HUMANPFKP118
V9GYV7V9GYV7_HUMANPFKP113
Q5VSR5Q5VSR5_HUMANPFKP210
B1APP6B1APP6_HUMANPFKP568
A0A8V8TMY4A0A8V8TMY4_HUMANPFKP835
A0A7I2YQB6A0A7I2YQB6_HUMANPFKP52
A0A7I2V5S1A0A7I2V5S1_HUMANPFKP122

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL451164
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL731533
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF455188
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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