P08679 · CISY2_YEAST
- ProteinCitrate synthase, peroxisomal
- GeneCIT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids460 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Peroxisomal citrate synthase involved in the citrate homeostasis (PubMed:25982115, PubMed:3023912).
Catalyzes the condensation of acetyl coenzyme A and oxaloacetate to form citrate (PubMed:25982115, PubMed:3023912).
Citrate synthase is the rate-limiting enzyme of the tricarboxylic acid (TCA) cycle (Probable)
Catalyzes the condensation of acetyl coenzyme A and oxaloacetate to form citrate (PubMed:25982115, PubMed:3023912).
Citrate synthase is the rate-limiting enzyme of the tricarboxylic acid (TCA) cycle (Probable)
Miscellaneous
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Present with 2310 molecules/cell in log phase SD medium.
Catalytic activity
- acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H+
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 293 | |||||
Sequence: H | ||||||
Active site | 339 | |||||
Sequence: H | ||||||
Active site | 394 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | peroxisome | |
Molecular Function | citrate (Si)-synthase activity | |
Molecular Function | identical protein binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | citrate metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCitrate synthase, peroxisomal
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP08679
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Leads to glutamate auxotrophy and poor growth on rich medium containing lactate, a nonfermentable carbon source, when CIT1 is also deleted.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 293 | Prevents the stabilization of the enzyme by oxaloacetate and impairs the catalytic activity. | ||||
Sequence: H → G | ||||||
Mutagenesis | 294 | Leads to a decrease of the catalytic activity and the ubiquitination efficiency. | ||||
Sequence: G → A or V | ||||||
Mutagenesis | 339 | Prevents the stabilization of the enzyme by oxaloacetate and impairs the catalytic activity. | ||||
Sequence: H → Q or N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000169984 | 1-460 | Citrate synthase, peroxisomal | |||
Sequence: MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQVYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGEVPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQGISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKDEDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEVLEWLFALKEEVNDDYSKDTIEKYLWDTLNSGRVIPGYGHAVLRKTDPRYMAQRKFAMDHFPDYELFKLVSSIYEVAPGVLTEHGKTKNPWPNVDAHSGVLLQYYGLKESSFYTVLFGVSRAFGILAQLITDRAIGASIERPKSYSTEKYKELVKNIESKL | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 218 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 239 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 354 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 385 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(UCC1), which leads to its degradation by the proteasome (PubMed:25982115).
Ubiquitination is prevented by oxaloacetate, suggesting the existence of an oxaloacetate-dependent positive feedback loop that stabilizes CIT2 (PubMed:25982115).
Ubiquitination is prevented by oxaloacetate, suggesting the existence of an oxaloacetate-dependent positive feedback loop that stabilizes CIT2 (PubMed:25982115).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with F-box protein UCC1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08679 | CIT2 P08679 | 3 | EBI-4713, EBI-4713 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 458-460 | C-terminal peroxisome targeting signal (PTS1) | ||||
Sequence: SKL |
Sequence similarities
Belongs to the citrate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length460
- Mass (Da)51,413
- Last updated1988-01-01 v1
- ChecksumAB2F66AD9A9399EF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z11113 EMBL· GenBank· DDBJ | CAA77442.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M14686 EMBL· GenBank· DDBJ | AAA34497.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X59720 EMBL· GenBank· DDBJ | CAA42342.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692837 EMBL· GenBank· DDBJ | AAT92856.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M54982 EMBL· GenBank· DDBJ | AAA34498.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006937 EMBL· GenBank· DDBJ | DAA07484.1 EMBL· GenBank· DDBJ | Genomic DNA |