Q8TGA0 · PFKA2_PICPA
- ProteinATP-dependent 6-phosphofructokinase subunit beta
- GenePFK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids941 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H+
Cofactor
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 mM | D-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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 191 | ATP 1 (UniProtKB | ChEBI); substrate | ||||
Sequence: G | ||||||
Binding site | 255-256 | ATP 1 (UniProtKB | ChEBI); substrate | ||||
Sequence: RC | ||||||
Binding site | 285-288 | ATP 1 (UniProtKB | ChEBI); substrate | ||||
Sequence: GDGS | ||||||
Binding site | 286 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 331-333 | beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: SID | ||||||
Active site | 333 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 368 | beta-D-fructose 6-phosphate 1 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: R | ||||||
Binding site | 375-377 | beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: MGR | ||||||
Binding site | 395 | ATP 2 (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: I | ||||||
Binding site | 400-405 | ATP 2 (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: KPASSR | ||||||
Binding site | 410 | ATP 2 (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: Q | ||||||
Binding site | 432 | beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: E | ||||||
Binding site | 460 | beta-D-fructose 6-phosphate 1 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: R | ||||||
Binding site | 466-469 | beta-D-fructose 6-phosphate 2 (UniProtKB | ChEBI); ligand shared with subunit alpha | ||||
Sequence: HVQR | ||||||
Binding site | 557-558 | ATP 2 (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: NS | ||||||
Binding site | 643 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: R | ||||||
Binding site | 701-705 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: TISNN | ||||||
Binding site | 739 | beta-D-fructose 2,6-bisphosphate 1 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: R | ||||||
Binding site | 746-748 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: QGG | ||||||
Binding site | 806 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: E | ||||||
Binding site | 832 | beta-D-fructose 2,6-bisphosphate 1 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: K | ||||||
Binding site | 838-841 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: HVQQ | ||||||
Binding site | 918 | beta-D-fructose 2,6-bisphosphate 2 (UniProtKB | ChEBI); allosteric activator; ligand shared with subunit alpha | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Cellular Component | mitochondrion | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | monosaccharide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase subunit beta
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Komagataella
Accessions
- Primary accessionQ8TGA0
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000429716 | 2-941 | ATP-dependent 6-phosphofructokinase subunit beta | |||
Sequence: PDASLFNGTSFITLFAPNISLLQASIDFYTNFLGFAIRKNSNQKLFWLQLEEDQNNVSIQLILDPEHAASVSQIDQNIRNLTRSLYRKDWRSIQSNIAFKSSSLSKLVKLLKDGGHPVQQSPNEISPFEVYTVDPLGSLIGFSGFKNPFAVNERSLLPKVSEEKAYRAEDDSEKLLNPVRKTIGVMTSGGDSPGMNPFVRAVVRAGIYKGCKVFCIHEGYEGLVRGGEKYIKETQWHDVRGWLVEGGTNIGTARCKEFRERSGRLKACKNMIDMGIDALIVCGGDGSLTGADRFRSEWPSLIEELLQTEQISQQQFNTHQNLNICGAVGSIDNDMSSTDATIGAFSSLDRICRAIDYIDATANSHSRAFIVEVMGRHCGWLGLLAGLATSADYILIPEKPASSREWQDQMCDIVGKHRARGKRKTIVIVAEGAISNDLSPISCDQVKDVLVNRLGLDTRVTTLGHVQRGGTAVAFDRIYATLQGVEAVNAVLECDADTPSPMIAIKEDQITRVPLVDAVELTQQVAKSIESRNFKKAISLRDSEFVEHMKNFISTNSADHVPPSLPLEKRKKIAIINVGAPAGGMNSAVYSMATYCMSRGHVPYAIHNGFSGLARHESVRSINWLDIEGWGSLGGSEIGTNRTLPNDADIGMIAYFFEKYGFDGLILVGGFEAFISLHQLERARINYPSLRIPLVLIPATISNNVPGTEYSLGSDTCLNSFMEYCDVIKQSAAATRNRVFVVEVQGGNSGYIATHAQLACGAQISYVPEEGISLAQLEMDINSLKESFANDQGKTKSGRLILKSENASKVLTTEVISTIIDDEASGRFDSKTAIPGHVQQGGIPSPMDRVRASRFAIRAVSFIERHSDRCQTFKNSISFRQTDEITSTAVVLGIHKSQLRFTPIRQLYDFESDVPRRMRKNIFWSNVREISDMLSGRTSL |
Interaction
Subunit
Heterododecamer of 4 alpha, 4 beta and 4 gamma chains.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-558 | N-terminal catalytic PFK domain 1 | ||||
Sequence: PDASLFNGTSFITLFAPNISLLQASIDFYTNFLGFAIRKNSNQKLFWLQLEEDQNNVSIQLILDPEHAASVSQIDQNIRNLTRSLYRKDWRSIQSNIAFKSSSLSKLVKLLKDGGHPVQQSPNEISPFEVYTVDPLGSLIGFSGFKNPFAVNERSLLPKVSEEKAYRAEDDSEKLLNPVRKTIGVMTSGGDSPGMNPFVRAVVRAGIYKGCKVFCIHEGYEGLVRGGEKYIKETQWHDVRGWLVEGGTNIGTARCKEFRERSGRLKACKNMIDMGIDALIVCGGDGSLTGADRFRSEWPSLIEELLQTEQISQQQFNTHQNLNICGAVGSIDNDMSSTDATIGAFSSLDRICRAIDYIDATANSHSRAFIVEVMGRHCGWLGLLAGLATSADYILIPEKPASSREWQDQMCDIVGKHRARGKRKTIVIVAEGAISNDLSPISCDQVKDVLVNRLGLDTRVTTLGHVQRGGTAVAFDRIYATLQGVEAVNAVLECDADTPSPMIAIKEDQITRVPLVDAVELTQQVAKSIESRNFKKAISLRDSEFVEHMKNFISTNS | ||||||
Region | 559-572 | Interdomain linker | ||||
Sequence: ADHVPPSLPLEKRK | ||||||
Region | 573-941 | C-terminal regulatory PFK domain 2 | ||||
Sequence: KIAIINVGAPAGGMNSAVYSMATYCMSRGHVPYAIHNGFSGLARHESVRSINWLDIEGWGSLGGSEIGTNRTLPNDADIGMIAYFFEKYGFDGLILVGGFEAFISLHQLERARINYPSLRIPLVLIPATISNNVPGTEYSLGSDTCLNSFMEYCDVIKQSAAATRNRVFVVEVQGGNSGYIATHAQLACGAQISYVPEEGISLAQLEMDINSLKESFANDQGKTKSGRLILKSENASKVLTTEVISTIIDDEASGRFDSKTAIPGHVQQGGIPSPMDRVRASRFAIRAVSFIERHSDRCQTFKNSISFRQTDEITSTAVVLGIHKSQLRFTPIRQLYDFESDVPRRMRKNIFWSNVREISDMLSGRTSL |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length941
- Mass (Da)103,733
- Last updated2002-06-01 v1
- ChecksumBA5FCF3DE48C5899
Keywords
- Technical term