P00905 · TRPGD_SALTY
- ProteinBifunctional protein TrpGD
- GenetrpGD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids531 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.
Catalytic activity
- chorismate + L-glutamine = anthranilate + H+ + L-glutamate + pyruvate
Activity regulation
Cooperatively feedback inhibited by tryptophan.
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 2/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57-59 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: GPG | ||||||
Active site | 84 | Nucleophile; for GATase activity | ||||
Sequence: C | ||||||
Binding site | 88 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 134-135 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Active site | 170 | For GATase activity | ||||
Sequence: H | ||||||
Active site | 172 | For GATase activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | anthranilate phosphoribosyltransferase activity | |
Molecular Function | anthranilate synthase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | glutamine metabolic process | |
Biological Process | phenazine biosynthetic process | |
Biological Process | tryptophan biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein TrpGD
Including 2 domains:
- Recommended nameAnthranilate synthase component 2
- EC number
- Short namesAS; ASII
- Alternative names
- Recommended nameAnthranilate phosphoribosyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP00905
Proteomes
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000056897 | 2-531 | Bifunctional protein TrpGD | |||
Sequence: ADILLLDNIDSFTWNLADQLRTNGHNVVIYRNHIPAQTLIDRLATMKNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNVPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLTQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPEYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGLRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQDQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGQEDLKANAQTVLDVLRNGTAYDRVTALAARG |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-196 | Glutamine amidotransferase type-1 | ||||
Sequence: DILLLDNIDSFTWNLADQLRTNGHNVVIYRNHIPAQTLIDRLATMKNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNVPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEP | ||||||
Region | 202-531 | Anthranilate phosphoribosyltransferase | ||||
Sequence: PILEKLYQAQTLTQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPEYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGLRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQDQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGQEDLKANAQTVLDVLRNGTAYDRVTALAARG |
Sequence similarities
In the C-terminal section; belongs to the anthranilate phosphoribosyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length531
- Mass (Da)56,918
- Last updated2007-01-23 v4
- Checksum256D2409062CD4C7
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 191-192 | in Ref. 3; AAA57312 | ||||
Sequence: QQ → LA | ||||||
Sequence conflict | 511 | in Ref. 1; AAA27236 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AH000942 EMBL· GenBank· DDBJ | AAA27236.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL20642.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J01811 EMBL· GenBank· DDBJ | AAA57312.1 EMBL· GenBank· DDBJ | Genomic DNA |