Q5R9C1 · F263_PONAB

Function

function

Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activity

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site42-50ATP (UniProtKB | ChEBI)
Binding site75beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Binding site99beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Active site125
Binding site127beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Binding site133beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Active site155
Binding site164-169ATP (UniProtKB | ChEBI)
Binding site169beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Binding site190beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Binding site194beta-D-fructose 6-phosphate (UniProtKB | ChEBI)
Binding site253beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Site253Transition state stabilizer
Active site254Tele-phosphohistidine intermediate
Binding site260beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Site260Transition state stabilizer
Binding site266beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Active site323Proton donor/acceptor
Binding site334beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Binding site345-348ATP (UniProtKB | ChEBI)
Binding site348beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Binding site352beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Binding site363beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Site388Transition state stabilizer
Binding site389beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Binding site389-393ATP (UniProtKB | ChEBI)
Binding site393beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI)
Binding site425ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function6-phosphofructo-2-kinase activity
Molecular FunctionATP binding
Molecular Functionfructose-2,6-bisphosphate 2-phosphatase activity
Biological Processfructose 2,6-bisphosphate metabolic process
Biological Processfructose metabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
  • Short names
    6PF-2-K/Fru-2,6-P2ase 3; PFK/FBPase 3
  • Alternative names
    • 6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme

Including 2 domains:

  • Recommended name
    6-phosphofructo-2-kinase
  • EC number
  • Recommended name
    Fructose-2,6-bisphosphatase
  • EC number

Gene names

    • Name
      PFKFB3

Organism names

Accessions

  • Primary accession
    Q5R9C1
  • Secondary accessions
    • Q5R404
    • Q5R5L4

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003451491-5146-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Modified residue461Phosphoserine; by AMPK and PKA
Modified residue463Phosphothreonine
Modified residue467Phosphoserine
Modified residue471Phosphothreonine; by PKC

Post-translational modification

Phosphorylation by AMPK stimulates activity.

Keywords

Interaction

Subunit

Homodimer. Forms a heterodimer with PFKFB2 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-2456-phosphofructo-2-kinase
Region246-514Fructose-2,6-bisphosphatase
Region444-475Disordered

Sequence similarities

In the C-terminal section; belongs to the phosphoglycerate mutase family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q5R9C1-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    514
  • Mass (Da)
    58,876
  • Last updated
    2008-07-22 v2
  • Checksum
    18FD1D267306853D
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQPLLGQACLT

Q5R9C1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 3-26: LELTQSRVQKIWVPVDHRPSLPRS → FRKA
    • 506-514: PLLGQACLT → NMKGSRSSADSSRKH

Q5R9C1-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 3-26: LELTQSRVQKIWVPVDHRPSLPRS → FRKA
    • 514-514: T → RTVCHIFSKFSPY

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A6D2XVH3A0A6D2XVH3_PONABPFKFB3526
A0A2J8VK41A0A2J8VK41_PONABPFKFB3568
A0A2J8VK47A0A2J8VK47_PONABPFKFB3534
A0A2J8VK48A0A2J8VK48_PONABPFKFB3455
A0A2J8VK62A0A2J8VK62_PONABPFKFB3520

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0349193-26in isoform 2 and isoform 3
Sequence conflict37in Ref. 1; CAH92952
Sequence conflict224in Ref. 1; CAH93512
Sequence conflict326in Ref. 1; CAH91639
Alternative sequenceVSP_034920506-514in isoform 2
Alternative sequenceVSP_034921514in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR859468
EMBL· GenBank· DDBJ
CAH91639.1
EMBL· GenBank· DDBJ
mRNA
CR860843
EMBL· GenBank· DDBJ
CAH92952.1
EMBL· GenBank· DDBJ
mRNA
CR861456
EMBL· GenBank· DDBJ
CAH93512.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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