P00937 · TRPG_YEAST
- ProteinMultifunctional tryptophan biosynthesis protein
- GeneTRP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids484 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Miscellaneous
Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
Yeast component II C-terminal half also has indole-3-glycerol phosphate synthase activity.
Present with 13400 molecules/cell in log phase SD medium.
Catalytic activity
- chorismate + L-glutamine = anthranilate + H+ + L-glutamate + pyruvate
Pathway
Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64-66 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: GPG | ||||||
Active site | 92 | Nucleophile; for GATase activity | ||||
Sequence: C | ||||||
Binding site | 96 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 142-143 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Active site | 181 | For GATase activity | ||||
Sequence: H | ||||||
Active site | 183 | For GATase activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | anthranilate synthase complex | |
Cellular Component | cytoplasm | |
Molecular Function | anthranilate synthase activity | |
Molecular Function | indole-3-glycerol-phosphate synthase activity | |
Biological Process | glutamine metabolic process | |
Biological Process | tryptophan biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional tryptophan biosynthesis protein
Including 2 domains:
- Recommended nameAnthranilate synthase component 2
- EC number
- Short namesAS
- Alternative names
- Recommended nameIndole-3-glycerol phosphate synthase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP00937
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056866 | 1-484 | Multifunctional tryptophan biosynthesis protein | |||
Sequence: MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By tryptophan starvation.
Interaction
Subunit
Tetramer of two components I and two components II.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P00937 | TRP2 P00899 | 4 | EBI-19585, EBI-19575 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-207 | Glutamine amidotransferase type-1 | ||||
Sequence: HVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEE | ||||||
Region | 215-484 | Indole-3-glycerol phosphate synthase | ||||
Sequence: SILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length484
- Mass (Da)53,489
- Last updated1994-06-01 v2
- Checksum34EF65E829279C1F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 32 | in Ref. 5; AAA34450 | ||||
Sequence: C → S | ||||||
Sequence conflict | 63-65 | in Ref. 5; AAA34450 | ||||
Sequence: PGP → LGL | ||||||
Sequence conflict | 129 | in Ref. 1; AAA35176 | ||||
Sequence: K → R | ||||||
Sequence conflict | 170 | in Ref. 5; AAA34450 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 236 | in Ref. 5; AAA34450 | ||||
Sequence: G → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
K01386 EMBL· GenBank· DDBJ | AAA35176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X75951 EMBL· GenBank· DDBJ | CAA53562.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28211 EMBL· GenBank· DDBJ | CAA82056.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M36300 EMBL· GenBank· DDBJ | AAA34450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA08958.1 EMBL· GenBank· DDBJ | Genomic DNA |