Q8TGA0 · PFKA2_PICPA

Function

function

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

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.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
6.971 mMD-fructose 6-phosphate

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 site191ATP 1 (UniProtKB | ChEBI); substrate
Binding site255-256ATP 1 (UniProtKB | ChEBI); substrate
Binding site285-288ATP 1 (UniProtKB | ChEBI); substrate
Binding site286Mg2+ (UniProtKB | ChEBI); catalytic
Binding site331-333beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha
Active site333Proton acceptor
Binding site368beta-D-fructose 6-phosphate 1 (UniProtKB | ChEBI); ligand shared with subunit alpha
Binding site375-377beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha
Binding site395ATP 2 (UniProtKB | ChEBI); allosteric inhibitor
Binding site400-405ATP 2 (UniProtKB | ChEBI); allosteric inhibitor
Binding site410ATP 2 (UniProtKB | ChEBI); allosteric inhibitor
Binding site432beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha
Binding site460beta-D-fructose 6-phosphate 1 (UniProtKB | ChEBI); ligand shared with subunit alpha
Binding site466-469beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha
Binding site557-558ATP 2 (UniProtKB | ChEBI); allosteric inhibitor
Binding site643beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site701-705beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site739beta-D-fructose 2,6-bisphosphate 1 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site746-748beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site806beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site832beta-D-fructose 2,6-bisphosphate 1 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site838-841beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha
Binding site918beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha

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 subunit beta
  • EC number
  • Alternative names
    • ATP-dependent 6-phosphofructokinase 2
      (ATP-PFK 2
      ; Phosphofructokinase 2
      )
    • Phosphohexokinase 2

Gene names

    • Name
      PFK2

Organism names

Accessions

  • Primary accession
    Q8TGA0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004297162-941ATP-dependent 6-phosphofructokinase subunit beta

Interaction

Subunit

Heterododecamer of 4 alpha, 4 beta and 4 gamma chains.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region2-558N-terminal catalytic PFK domain 1
Region559-572Interdomain linker
Region573-941C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    941
  • Mass (Da)
    103,733
  • Last updated
    2002-06-01 v1
  • Checksum
    BA5FCF3DE48C5899
MPDASLFNGTSFITLFAPNISLLQASIDFYTNFLGFAIRKNSNQKLFWLQLEEDQNNVSIQLILDPEHAASVSQIDQNIRNLTRSLYRKDWRSIQSNIAFKSSSLSKLVKLLKDGGHPVQQSPNEISPFEVYTVDPLGSLIGFSGFKNPFAVNERSLLPKVSEEKAYRAEDDSEKLLNPVRKTIGVMTSGGDSPGMNPFVRAVVRAGIYKGCKVFCIHEGYEGLVRGGEKYIKETQWHDVRGWLVEGGTNIGTARCKEFRERSGRLKACKNMIDMGIDALIVCGGDGSLTGADRFRSEWPSLIEELLQTEQISQQQFNTHQNLNICGAVGSIDNDMSSTDATIGAFSSLDRICRAIDYIDATANSHSRAFIVEVMGRHCGWLGLLAGLATSADYILIPEKPASSREWQDQMCDIVGKHRARGKRKTIVIVAEGAISNDLSPISCDQVKDVLVNRLGLDTRVTTLGHVQRGGTAVAFDRIYATLQGVEAVNAVLECDADTPSPMIAIKEDQITRVPLVDAVELTQQVAKSIESRNFKKAISLRDSEFVEHMKNFISTNSADHVPPSLPLEKRKKIAIINVGAPAGGMNSAVYSMATYCMSRGHVPYAIHNGFSGLARHESVRSINWLDIEGWGSLGGSEIGTNRTLPNDADIGMIAYFFEKYGFDGLILVGGFEAFISLHQLERARINYPSLRIPLVLIPATISNNVPGTEYSLGSDTCLNSFMEYCDVIKQSAAATRNRVFVVEVQGGNSGYIATHAQLACGAQISYVPEEGISLAQLEMDINSLKESFANDQGKTKSGRLILKSENASKVLTTEVISTIIDDEASGRFDSKTAIPGHVQQGGIPSPMDRVRASRFAIRAVSFIERHSDRCQTFKNSISFRQTDEITSTAVVLGIHKSQLRFTPIRQLYDFESDVPRRMRKNIFWSNVREISDMLSGRTSL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF395078
EMBL· GenBank· DDBJ
AAL82590.2
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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