A0A496PB39 · A0A496PB39_9FIRM
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids319 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+
Cofactor
Activity regulation
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
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 | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 21-25 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RAITR | ||||||
Binding site | 72-73 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RY | ||||||
Binding site | 102-105 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 125-127 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 127 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 154 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 162 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 169-171 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 185-187 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: GAE | ||||||
Binding site | 213-215 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: KEY | ||||||
Binding site | 222 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 249-252 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: YLQR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
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
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Bacillota > Negativicutes > Veillonellales > Veillonellaceae > Veillonella
Accessions
- Primary accessionA0A496PB39
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-275 | Phosphofructokinase | ||||
Sequence: KIALLTSGGDAPGMNAAIRAITRKAIHEGFSVYGIERGFEGIINSEIRPLHARDVGGIITTGGTILRTARYPEFKNLDVQQRAYRILQDFGIDHLIVIGGDGSQAGAEALMRLGQSTITIPCTIDNDMNGTQYTIGFDTALNTVVDAVGRIRDTSNSHERVAIIEVMGRHAGHIALQAGLASGAELVLVPEYPMPLDEVCEHINKTHQLGKEYSIILVAEGAYSSGEVKEYIKQHTYFDPSLTVLGYLQRGGAPSALDAILAACMSELAVDCL |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length319
- Mass (Da)34,544
- Last updated2019-06-05 v1
- Checksum1D15841C94E1C8D2