P33974 · TRPG_HALVD
- ProteinAnthranilate synthase component 2
- GenetrpG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids204 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic activity
- chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate + H+
Pathway
Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | anthranilate 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 nameAnthranilate synthase component 2
- EC number
- Short namesAS; ASII
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionP33974
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056883 | 1-204 | Anthranilate synthase component 2 | |||
Sequence: MIRLVVVDNFDSFTYNLVEYFSEQTVEGEPLDIEVRKNTASLDEIRDLDPDAIVISPGPGHPKNDRDVGVTNDVLTELSTEIPTLGVCLGLEAAVYAYGGTIGHAPEPIHGKAFPVDHDGAGVFAGLEDGFPAGRYHSLVATDVPDCFDVSATTDHDGEALVMGVRHRDYPIECVQFHPESVLTGSGHGVVRNFLTAVAGFDVA |
Proteomic databases
Interaction
Subunit
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-204 | Glutamine amidotransferase type-1 | ||||
Sequence: RLVVVDNFDSFTYNLVEYFSEQTVEGEPLDIEVRKNTASLDEIRDLDPDAIVISPGPGHPKNDRDVGVTNDVLTELSTEIPTLGVCLGLEAAVYAYGGTIGHAPEPIHGKAFPVDHDGAGVFAGLEDGFPAGRYHSLVATDVPDCFDVSATTDHDGEALVMGVRHRDYPIECVQFHPESVLTGSGHGVVRNFLTAVAGFDVA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length204
- Mass (Da)21,849
- Last updated2011-09-21 v2
- Checksum6FC8FCE64599C444
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 38 | in Ref. 1; AAA73178 | ||||
Sequence: N → T | ||||||
Sequence conflict | 107-108 | in Ref. 1; AAA73178 | ||||
Sequence: EP → DA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M83788 EMBL· GenBank· DDBJ | AAA73178.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001956 EMBL· GenBank· DDBJ | ADE03081.1 EMBL· GenBank· DDBJ | Genomic DNA |