A0A974BW21 · A0A974BW21_XENLA
- ProteinATP-citrate synthase
- Geneacly.L
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1091 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
Catalytic activity
- oxaloacetate + acetyl-CoA + ADP + phosphate = citrate + ATP + CoAThis reaction proceeds in the backward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 750 | Tele-phosphohistidine intermediate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ATP citrate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | acetyl-CoA biosynthetic process | |
Biological Process | citrate metabolic process | |
Biological Process | fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-citrate synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA0A974BW21
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 441-461 | Polar residues | ||||
Sequence: ASGSSSTPAPSRTASFSESRT | ||||||
Region | 441-472 | Disordered | ||||
Sequence: ASGSSSTPAPSRTASFSESRTEDITPAKKSKP | ||||||
Domain | 482-591 | CoA-binding | ||||
Sequence: LFTRHTKSIVWGMQTRAVQGMLDFDYICSRSEPSVAALVYPFTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDVLINFASLRSAYDSTIETMNFPQIRAIAIIAEGI |
Sequence similarities
In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.
In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,091
- Mass (Da)119,860
- Last updated2023-02-22 v1
- ChecksumAC1C3045510437E6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 441-461 | Polar residues | ||||
Sequence: ASGSSSTPAPSRTASFSESRT |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM004482 EMBL· GenBank· DDBJ | OCT62009.1 EMBL· GenBank· DDBJ | Genomic DNA |