A0A142EQH9 · A0A142EQH9_9BACT
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (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
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + 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 | 22 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 32-36 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: RAAVR | ||||||
Binding site | 83-84 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 113-116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGT | ||||||
Binding site | 114 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 137-139 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 139 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 166 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 174 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 181-183 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 197-199 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: GAE | ||||||
Binding site | 222 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 224-226 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: KTS | ||||||
Binding site | 233 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 259 | substrate; ligand shared between dimeric partners | ||||
Sequence: K | ||||||
Binding site | 265-268 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HIQR |
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
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Cytophagia > Cytophagales > Cyclobacteriaceae > Algoriphagus
Accessions
- Primary accessionA0A142EQH9
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-290 | Phosphofructokinase | ||||
Sequence: KIAVFTSGGDSPGMNACIRAAVRTGIYKGLDVFGIYRGYEGMIEGDIKRLHSHSVSNIIQRGGTVLKSARSMEFKTPEGRKKAFENLSAHGIEGLVAIGGDGTFTGAKVFYEEFGIPTVGCPGTIDNDIYGTDYTIGFDTAVNTALEAIDKIRDTAAAHDRIFFIEVMGRDAGFIAVESGIGGGAEFVMVPETQTDLDAVVKSLKKLRKTKTSSIIVVAEGDDLGSADVIMKLVKEKIQDPSKEFKVTTLGHIQRGGNPTARDRVLGSRCGMAAVEG |
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
- Length335
- Mass (Da)35,723
- Last updated2016-06-08 v1
- ChecksumA42FEDAB8D902A3E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP012836 EMBL· GenBank· DDBJ | AMQ57384.1 EMBL· GenBank· DDBJ | Genomic DNA |