Protein profile

PA5142

imidazole glycerol phosphate synthase subunit HisH

Genome: NC_002516.2

Gene: PA5142 hisH1 Structure source: AlphaFold UniProt Q9HU42
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Amino acids 213
Annotations 8
Features 18
PDB binders 1

Overview

Basic information about this protein and its source genome.

Accession
PA5142
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5142 hisH1
Status
annotated
Amino acids
213
Structure source
AlphaFold
EC
4.3.2.10 3.5.1.2
GO
GO:0009382 Complex that possesses imidazoleglycerol-phosphate synthase activity. GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+. GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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.

2 EC 6 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

6
  • GO:0009382 Complex that possesses imidazoleglycerol-phosphate synthase activity.
  • GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
  • GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+.
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
  • GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
  • GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
3 211 PIRSF PIRSF000495 Amidotransf_HisH
3 211 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
4 213 ProSiteProfiles PS51273 Glutamine amidotransferase type 1 domain profile.
5 208 NCBIfam TIGR01855 imidazole glycerol phosphate synthase subunit HisH
5 208 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
3 208 PANTHER PTHR42701 IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH
3 208 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
2 212 FunFam G3DSA:3.40.50.880:FF:000023 Imidazole glycerol phosphate synthase subunit HisH
7 207 Pfam PF00117 Glutamine amidotransferase class-I
7 207 InterPro IPR017926 Glutamine amidotransferase
1 212 Gene3D G3DSA:3.40.50.880 -
1 212 InterPro IPR029062 Class I glutamine amidotransferase-like
5 207 CDD cd01748 GATase1_IGP_Synthase
5 207 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
4 209 Hamap MF_00278 Imidazole glycerol phosphate synthase subunit HisH [hisH].
4 209 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
2 209 SUPERFAMILY SSF52317 Class I glutamine amidotransferase-like
2 209 InterPro IPR029062 Class I glutamine amidotransferase-like

3D Structure

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

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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 PA5142
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.

51 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
GUO
7AC8
Q9X0C8 577.3 Da LogP -4.48 TPSA 318.2 3 viol. ✓ Clean c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=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.