Protein profile

PA0975

radical activating enzyme

Genome: NC_002516.2

Gene: queE PA0975 Structure source: AlphaFold UniProt Q9I4Z3
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Amino acids 264
Annotations 8
Features 16
PDB binders 1

Overview

Basic information about this protein and its source genome.

Accession
PA0975
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
queE PA0975
Status
annotated
Amino acids
264
Structure source
AlphaFold
EC
4.3.99.3
GO
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0016840 Catalysis of the release of ammonia or one of its derivatives, with the formation of a double bond or ring. Enzymes with this activity may catalyze the actual elimination of the ammonia, amine or amide, e.g. CH-CH(-NH-R) = C=CH- + NH2-R. Others, however, catalyze elimination of another component, e.g. water, which is followed by spontaneous reactions that lead to breakage of the C-N bond, e.g. L-serine ammonia-lyase (EC:4.3.1.17), so that the overall reaction is C(-OH)-CH(-NH2) = CH2-CO- + NH4+, i.e. an elimination with rearrangement. The sub-subclasses of EC:4.3 are the ammonia-lyases (EC:4.3.1), lyases acting on amides, amidines, etc. (EC:4.3.2), the amine-lyases (EC:4.3.3), and other carbon-nitrogen lyases (EC:4.3.99). GO:0000287 Binding to a magnesium (Mg) ion. GO:1904047 Binding to S-adenosyl-L-methionine. GO:0008616 The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in position 34 of tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon. 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
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Sequence

Primary amino-acid sequence viewer.

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:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0016840 Catalysis of the release of ammonia or one of its derivatives, with the formation of a double bond or ring. Enzymes with this activity may catalyze the actual elimination of the ammonia, amine or amide, e.g. CH-CH(-NH-R) = C=CH- + NH2-R. Others, however, catalyze elimination of another component, e.g. water, which is followed by spontaneous reactions that lead to breakage of the C-N bond, e.g. L-serine ammonia-lyase (EC:4.3.1.17), so that the overall reaction is C(-OH)-CH(-NH2) = CH2-CO- + NH4+, i.e. an elimination with rearrangement. The sub-subclasses of EC:4.3 are the ammonia-lyases (EC:4.3.1), lyases acting on amides, amidines, etc. (EC:4.3.2), the amine-lyases (EC:4.3.3), and other carbon-nitrogen lyases (EC:4.3.99).
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:1904047 Binding to S-adenosyl-L-methionine.
  • GO:0008616 The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in position 34 of tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon.
  • 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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
69 260 ProSiteProfiles PS51918 Radical SAM core domain profile.
69 260 InterPro IPR007197 Radical SAM
77 215 SFLD SFLDS00029 Radical SAM
77 215 InterPro IPR007197 Radical SAM
50 263 PANTHER PTHR42836 7-CARBOXY-7-DEAZAGUANINE SYNTHASE
80 153 CDD cd01335 Radical_SAM
53 258 Gene3D G3DSA:3.20.20.70 Aldolase class I
53 258 InterPro IPR013785 Aldolase-type TIM barrel
75 156 Pfam PF13394 4Fe-4S single cluster domain
76 154 SUPERFAMILY SSF102114 Radical SAM enzymes
54 261 Hamap MF_00917 7-carboxy-7-deazaguanine synthase [queE].
54 261 InterPro IPR024924 7-carboxy-7-deazaguanine synthase-like
77 197 Pfam PF04055 Radical SAM superfamily
77 197 InterPro IPR007197 Radical SAM
54 264 NCBIfam TIGR04349 7-carboxy-7-deazaguanine synthase QueE
54 264 InterPro IPR027621 Putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE

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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA0975
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
7C5
5TH5
O31677 456.4 Da LogP -2.51 TPSA 243.2 1 viol. ✓ Clean c1c(nc2c(n1)NC(=NC2=O)N)C(=O)OC[C@@H]3[C@H]([C@…

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.