Protein profile

PA5098

histidine ammonia-lyase

Genome: NC_002516.2

Gene: hutH PA5098 Structure source: AlphaFold UniProt Q9HU85
Export view
Amino acids 509
Annotations 8
Features 20
PDB binders 9
Druggability 0.664

Overview

Basic information about this protein and its source genome.

Accession
PA5098
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
hutH PA5098
Status
annotated
Amino acids
509
Structure source
AlphaFold
EC
4.3.1.3
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004397 Catalysis of the reaction: L-histidine = trans-urocanate + NH4+. GO:0006548 The chemical reactions and pathways resulting in the breakdown of L-histidine. GO:0019556 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formamide. GO:0019557 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formate. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
54.348
Human E-value
7.61e-41
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.664
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSLHLKPGQLTLADLRQAYLAPVRLSLDPSADAPIAASVACVENIIAEGRTAYGINTGFGLLASTRISPADLEKLQRSIVLSHAAGVGEALDDAMVRLVMLLKVNSLARGFSGIRRKVIDALIALINAEVYPHIPLKGSVGASGDLAPLAHMSLVLIGESRARHRGEWLPAAEALAVAGLEPLTLAAKEGLALLNGTQVSTAYALRGLFEAEDLFAAATVCGGLSVEAMLGSRAPFDARIHAARGQRGQIDVAAAYRDLLTASSEVARSHEKCDKVQDPYSLRCQPQVMGACLTQMRQAAEVLEIEANAVSDNPLVFAAEGDVISGGNFHAEPVAMAADNLALALAEIGSLSERRISLMMDMHMSQLPPFLVANGGVNSGFMIAQVTAAALASDNKALAHPASVDSLPTSANQEDHVSMAPNAGKRLWAMAENVRGILAVEWLGACQGLDFREGLKSSPKLEQARRLLRDKVPYYQEDRFFAPDIEAASQLLASGCLNALLPARLLPSL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0004397 Catalysis of the reaction: L-histidine = trans-urocanate + NH4+.
  • GO:0006548 The chemical reactions and pathways resulting in the breakdown of L-histidine.
  • GO:0019556 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formamide.
  • GO:0019557 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formate.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0016841 Catalysis of the release of ammonia by the cleavage of a carbon-nitrogen bond or the reverse reaction with ammonia as a substrate.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
138 154 ProSitePatterns PS00488 Phenylalanine and histidine ammonia-lyases signature.
138 154 InterPro IPR022313 Phenylalanine/histidine ammonia-lyases, active site
293 313 Coils Coil Coil
2 196 Gene3D G3DSA:1.10.275.10 -
2 196 InterPro IPR024083 Fumarase/histidase, N-terminal
197 508 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
1 196 FunFam G3DSA:1.10.275.10:FF:000005 Histidine ammonia-lyase
10 469 Pfam PF00221 Aromatic amino acid lyase
10 469 InterPro IPR001106 Aromatic amino acid lyase
197 505 FunFam G3DSA:1.20.200.10:FF:000003 Histidine ammonia-lyase
8 452 CDD cd00332 PAL-HAL
8 452 InterPro IPR001106 Aromatic amino acid lyase
5 458 PANTHER PTHR10362 HISTIDINE AMMONIA-LYASE
5 458 InterPro IPR001106 Aromatic amino acid lyase
3 505 SUPERFAMILY SSF48557 L-aspartase-like
3 505 InterPro IPR008948 L-Aspartase-like
2 503 Hamap MF_00229 Histidine ammonia-lyase [hutH].
2 503 InterPro IPR005921 Histidine ammonia-lyase
4 507 NCBIfam TIGR01225 histidine ammonia-lyase
4 507 InterPro IPR005921 Histidine ammonia-lyase

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

Loading 3D structure...

Legend High Medium Low

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 PA5098
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
1 0.407
2 0.321

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.

59 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
247
2QVE
Q8GMG0 217.2 Da LogP 1.11 TPSA 83.5 ✓ Ro5 ✓ Clean c1cc(ccc1[C@H](C(C(=O)O)(F)F)N)O
295
2RJR
Q8GMG0 200.2 Da LogP 0.30 TPSA 77.8 ✓ Ro5 ✓ Clean c1cc(ccc1[C@@H]([C@@H](C(=O)O)O)O)F
296
2RJS
Q8GMG0 231.2 Da LogP 1.41 TPSA 72.5 ✓ Ro5 ✓ Clean COc1ccc(cc1)[C@H](C(C(=O)O)(F)F)N
DHC
2O7D
Q3IWB0 180.2 Da LogP 1.20 TPSA 77.8 ✓ Ro5 Alert c1cc(c(cc1\C=C\C(=O)O)O)O
HC4
2O7B
Q3IWB0 164.2 Da LogP 1.49 TPSA 57.5 ✓ Ro5 ✓ Clean c1cc(ccc1/C=C/C(=O)O)O
KZ5
6S7Q
M2BPW8 263.3 Da LogP -0.79 TPSA 123.6 ✓ Ro5 ✓ Clean CN(C)[C@@H](Cc1c[nH]c(n1)S(=O)(=O)O)C(=O)O
PMI
2O7E
Q3IWB0 213.2 Da LogP 0.62 TPSA 83.6 ✓ Ro5 ✓ Clean c1ccc2c(c1)CC(C2)(N)P(=O)(O)O
SFE
3UNV
Q84FL5 165.2 Da LogP 1.16 TPSA 63.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(CC(=O)O)N
TCA
2O78
Q3IWB0 148.2 Da LogP 1.78 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)\C=C\C(=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.