Protein profile

PA1989

coenzyme PQQ synthesis protein E

Genome: NC_002516.2

Gene: PA1989 pqqE Structure source: AlphaFold UniProt Q9I2C0
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Amino acids 381
Annotations 11
Features 29
PDB binders 1
Druggability 0.691

Overview

Basic information about this protein and its source genome.

Accession
PA1989
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1989 pqqE
Status
annotated
Amino acids
381
Structure source
AlphaFold
EC
1.21.98.4
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:0009975 Catalysis of a ring closure reaction. GO:0005506 Binding to an iron (Fe) ion. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:1904047 Binding to S-adenosyl-L-methionine. GO:0032324 The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.691
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MRNSGSSCSESVGPPLWLLAELTYRCPLQCPYCSNPLEFAREGAELSTAEWIEVFRQARELGAAQLGFSGGEPLLRQDLAELIEAGRGLGFYTNLITSGIGLDEARLARFAEAGLDHVQISFQAADEEVNNLLAGSRKAFAQKLAMARAVKAHGYPMVLNFVTHRHNIDNIERIIQLCIELEADYVELATCQFYGWAALNRAGLLPTRAQLERAERITAEYRQRLAAEGNPCKLIFVTPDYYEERPKACMGGWASVFLDITPDGTALPCHSARQLPVQFPNVREHSLRHIWYESFGFNRYRGDAWMPEPCRSCEEKERDHGGCRCQAFLLTGDADATDPVCAKSARHDLILAARRQAEEAPLGLDALTWRNQRASRLICKA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • 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:0009975 Catalysis of a ring closure reaction.
  • GO:0005506 Binding to an iron (Fe) ion.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:1904047 Binding to S-adenosyl-L-methionine.
  • GO:0032324 The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
  • GO:0018189 The chemical reactions and pathways resulting in the formation of the cofactor pyrroloquinoline quinone (PQQ); it is synthesized from a small peptide containing tyrosine and glutamic acid; these amino acids in the peptide are multiply cross-linked and the rest of the peptide is removed.
  • 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.
  • GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records
Show feature table
Start End DB Term Name
21 219 CDD cd01335 Radical_SAM
2 361 PIRSF PIRSF037420 PqqE
2 361 InterPro IPR017200 Coenzyme PQQ synthesis protein E-like
249 314 Pfam PF13186 Iron-sulfur cluster-binding domain
249 314 InterPro IPR023885 4Fe4S-binding SPASM domain
257 341 NCBIfam TIGR04085 SPASM domain
257 341 InterPro IPR023885 4Fe4S-binding SPASM domain
11 371 NCBIfam TIGR02109 pyrroloquinoline quinone biosynthesis protein PqqE
11 371 InterPro IPR011843 Coenzyme PQQ biosynthesis protein E, bacteria
16 219 SMART SM00729 MiaB
16 219 InterPro IPR006638 Elp3/MiaA/NifB-like, radical SAM core domain
25 83 Pfam PF13394 4Fe-4S single cluster domain
246 358 CDD cd21119 SPASM_PqqE
17 297 Gene3D G3DSA:3.20.20.70 Aldolase class I
17 297 InterPro IPR013785 Aldolase-type TIM barrel
9 378 SFLD SFLDS00029 Radical SAM
9 378 InterPro IPR007197 Radical SAM
14 323 SUPERFAMILY SSF102114 Radical SAM enzymes
12 228 ProSiteProfiles PS51918 Radical SAM core domain profile.
12 228 InterPro IPR007197 Radical SAM
2 341 PANTHER PTHR11228 RADICAL SAM DOMAIN PROTEIN
22 177 Pfam PF04055 Radical SAM superfamily
22 177 InterPro IPR007197 Radical SAM
9 378 SFLD SFLDF00280 coenzyme PQQ synthesis protein E (PqqE-like)
9 378 InterPro IPR011843 Coenzyme PQQ biosynthesis protein E, bacteria
1 381 Hamap MF_00660 PqqA peptide cyclase [pqqE].
1 381 InterPro IPR011843 Coenzyme PQQ biosynthesis protein E, bacteria
22 33 ProSitePatterns PS01305 moaA / nifB / pqqE family signature.
22 33 InterPro IPR000385 MoaA/NifB/PqqE, iron-sulphur binding, conserved site

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 PA1989
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 0.691

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
FES
6EFN
O31423 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1

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.