Protein profile

PA0649

anthranilate synthase component II

Genome: NC_002516.2

Gene: PA0649 trpG Structure source: AlphaFold UniProt P20576
Amino acids 201
Annotations 5
Features 24
PDB binders 3

Overview

Basic information about this protein and its source genome.

Accession
PA0649
Gene
PA0649 trpG
Status
annotated
Amino acids
201
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
28.8
Human E-value
7.82e-07
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0046820 Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
  • GO:0004049 Catalysis of the reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
  • GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate.
  • GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
47 56 PRINTS PR00097 Anthranilate synthase component II signature
169 182 PRINTS PR00097 Anthranilate synthase component II signature
99 107 PRINTS PR00097 Anthranilate synthase component II signature
2 16 PRINTS PR00097 Anthranilate synthase component II signature
119 131 PRINTS PR00097 Anthranilate synthase component II signature
74 85 PRINTS PR00097 Anthranilate synthase component II signature
1 199 ProSiteProfiles PS51273 Glutamine amidotransferase type 1 domain profile.
1 192 SUPERFAMILY SSF52317 Class I glutamine amidotransferase-like
1 192 InterPro IPR029062 Class I glutamine amidotransferase-like
1 193 Gene3D G3DSA:3.40.50.880 -
1 193 InterPro IPR029062 Class I glutamine amidotransferase-like
74 85 PRINTS PR00096 Glutamine amidotransferase superfamily signature
47 56 PRINTS PR00096 Glutamine amidotransferase superfamily signature
169 182 PRINTS PR00096 Glutamine amidotransferase superfamily signature
44 58 PRINTS PR00099 Carbamoyl-phosphate synthase protein GATase domain signature
74 90 PRINTS PR00099 Carbamoyl-phosphate synthase protein GATase domain signature
2 193 PANTHER PTHR43418 MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED
1 194 FunFam G3DSA:3.40.50.880:FF:000003 Anthranilate synthase component II
2 190 CDD cd01743 GATase1_Anthranilate_Synthase
2 190 InterPro IPR006221 Anthranilate synthase/para-aminobenzoate synthase like domain
4 191 Pfam PF00117 Glutamine amidotransferase class-I
4 191 InterPro IPR017926 Glutamine amidotransferase
1 191 NCBIfam TIGR00566 glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase
1 191 InterPro IPR006221 Anthranilate synthase/para-aminobenzoate synthase like domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

No pockets are loaded yet for the displayed AlphaFold model PA0649 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA0649
AlphaFold full sequence Viewing

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

53 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
IMP P0A6F1 348.2 Da LogP -2.15 TPSA 180.0 ✓ Ro5 ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…
ORN P0A6F1 132.2 Da LogP -0.86 TPSA 89.3 ✓ Ro5 ✓ Clean C(C[C@@H](C(=O)O)N)CN
POP P04079 176.0 Da LogP -2.08 TPSA 129.9 ✓ Ro5 ✓ Clean O[P@@](=O)([O-])O[P@@](=O)(O)[O-]

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.