U5H8Y7 · U5H8Y7_USTV1
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids859 (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, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
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 | 30 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 158-159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 188-191 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 189 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 234-236 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 236 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 271 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 278-280 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 335 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 363 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 369-372 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HTQR | ||||||
Binding site | 544 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 601-605 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 639 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 646-648 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGA | ||||||
Binding site | 706 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 732 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 811 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
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
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Microbotryomycetes > Microbotryales > Microbotryaceae > Microbotryum
Accessions
- Primary accessionU5H8Y7
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MGYSPHPSMPSSPTGGQG | ||||||
Region | 1-21 | Disordered | ||||
Sequence: MGYSPHPSMPSSPTGGQGRPT | ||||||
Region | 1-461 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MGYSPHPSMPSSPTGGQGRPTRLAVLTSGGDCSGMNAAVRAVVKMGISRGCEVYVVREGWEGLVRGNENEEPTTSQLTTSNLIPFNSTNAAAASANARPTERKPSRERGGFVATYGEGELLKEGEGEQTLRNRFILRVGWDDVRGFASLGGTLIGTARCAAFRELEGRRKAAFNLVKHGIDALVVCGGDGSLTGADRLRAEWPDHVQALLKSGQITPEQFEAHQHLNIVGLVGSIDNDMAGTDMTIGATTALHRICEAVDSISSTASSHSRAFVVEVMGRNCGWLALMAAIATGADYMFIPERPPTAEDWQTSMCTVLGRHRAEGKRKTIIIVAEGAHDCNLKPISPEEIKDVLTQRLGLDTRVTTLGHTQRGGAPAAYDRILATLQGAEAVEAVLASTVDSPSPVIGIQENKIQRQPLMEAVKKTQDVAKAIADKDFARALSLRDPEFEDCLHAFRATTR | ||||||
Domain | 22-69 | Phosphofructokinase | ||||
Sequence: RLAVLTSGGDCSGMNAAVRAVVKMGISRGCEVYVVREGWEGLVRGNEN | ||||||
Domain | 134-395 | Phosphofructokinase | ||||
Sequence: FILRVGWDDVRGFASLGGTLIGTARCAAFRELEGRRKAAFNLVKHGIDALVVCGGDGSLTGADRLRAEWPDHVQALLKSGQITPEQFEAHQHLNIVGLVGSIDNDMAGTDMTIGATTALHRICEAVDSISSTASSHSRAFVVEVMGRNCGWLALMAAIATGADYMFIPERPPTAEDWQTSMCTVLGRHRAEGKRKTIIIVAEGAHDCNLKPISPEEIKDVLTQRLGLDTRVTTLGHTQRGGAPAAYDRILATLQGAEAVEAV | ||||||
Domain | 475-764 | Phosphofructokinase | ||||
Sequence: RIAIIHTGAPAGGMNAATRTAVRYCLCHGHTPLAIYNGFVGLLHGNVAELSWLRVDQWSTRGGSELGTNRVLPDTDLAGVAAKLAEYKIDGLLIVGGFEAMVSLEQLEKGRKDHAALRIPLIHLPATISNNVPITEWSVGSDTSINVLVEACDSIKQSASASRNRVFVVETQGAGCGYIAMLGALATGANLVYTPENGISLGMLQRDVEFLKKRYSQDVAGKSEGRLIILSEKASKTYTTQVVTNIFAEEGKDSFDARSVALGHTLQGGVPSPRDRTRAIRLTVKCIDFL | ||||||
Region | 475-859 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RIAIIHTGAPAGGMNAATRTAVRYCLCHGHTPLAIYNGFVGLLHGNVAELSWLRVDQWSTRGGSELGTNRVLPDTDLAGVAAKLAEYKIDGLLIVGGFEAMVSLEQLEKGRKDHAALRIPLIHLPATISNNVPITEWSVGSDTSINVLVEACDSIKQSASASRNRVFVVETQGAGCGYIAMLGALATGANLVYTPENGISLGMLQRDVEFLKKRYSQDVAGKSEGRLIILSEKASKTYTTQVVTNIFAEEGKDSFDARSVALGHTLQGGVPSPRDRTRAIRLTVKCIDFLEKHHNQKLQNLAPDPQDPDAATIVIEGASIRFASLEEMVQAADFKNRRGKVQWWTSAKELVETMAGKKVPSEELKTPLTSPRTEKKDPNERFSRL | ||||||
Region | 830-859 | Disordered | ||||
Sequence: GKKVPSEELKTPLTSPRTEKKDPNERFSRL | ||||||
Compositional bias | 842-859 | Basic and acidic residues | ||||
Sequence: LTSPRTEKKDPNERFSRL |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.
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
- Length859
- Mass (Da)92,793
- Last updated2013-12-11 v1
- Checksum0B3A5549B6BA73ED
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MGYSPHPSMPSSPTGGQG | ||||||
Compositional bias | 842-859 | Basic and acidic residues | ||||
Sequence: LTSPRTEKKDPNERFSRL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AEIJ01000359 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
GL541678 EMBL· GenBank· DDBJ | KDE06000.1 EMBL· GenBank· DDBJ | Genomic DNA |