Protein profile

PA0510

uroporphyrin-III C-methyltransferase

Genome: NC_002516.2

Gene: cobA cysG_1 IPC1295_09180 nirE GUL26_18015 PA0510 PAERUG_P19_London_7_VIM_2_05_10_02002 DT376_23645 Structure source: Experimental + AlphaFold UniProt G3XD80 UniProt P95417
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Amino acids 279
Annotations 10
Features 19
PDB binders 4
Druggability 0.824

Overview

Basic information about this protein and its source genome.

Accession
PA0510
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
cobA cysG_1 IPC1295_09180 nirE GUL26_18015 PA0510 PAERUG_P19_London_7_VIM_2_05_10_02002 DT376_23645
Status
annotated
Amino acids
279
Structure source
Experimental + AlphaFold
EC
2.1.1.107
GO
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:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule. 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:0004851 Catalysis of the reaction: uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H+. GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor. GO:0009236 The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.824
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • 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:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
  • 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:0004851 Catalysis of the reaction: uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H+.
  • GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
  • GO:0009236 The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
  • GO:0006783 The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
  • GO:0032259 The process in which a methyl group is covalently attached to a molecule.
  • GO:0019354 The chemical reactions and pathways resulting in the formation of siroheme, a tetrahydroporphyrin with adjacent, reduced pyrrole rings.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
20 230 Pfam PF00590 Tetrapyrrole (Corrin/Porphyrin) Methylases
20 230 InterPro IPR000878 Tetrapyrrole methylase
134 266 FunFam G3DSA:3.30.950.10:FF:000001 Siroheme synthase
98 131 ProSitePatterns PS00840 Uroporphyrin-III C-methyltransferase signature 2.
98 131 InterPro IPR003043 Uroporphiryn-III C-methyltransferase, conserved site
14 263 SUPERFAMILY SSF53790 Tetrapyrrole methylase
14 263 InterPro IPR035996 Tetrapyrrole methylase superfamily
14 133 FunFam G3DSA:3.40.1010.10:FF:000001 Siroheme synthase
23 37 ProSitePatterns PS00839 Uroporphyrin-III C-methyltransferase signature 1.
23 37 InterPro IPR003043 Uroporphiryn-III C-methyltransferase, conserved site
134 266 Gene3D G3DSA:3.30.950.10 -
134 266 InterPro IPR014776 Tetrapyrrole methylase, subdomain 2
17 254 PANTHER PTHR45790 SIROHEME SYNTHASE-RELATED
18 253 NCBIfam TIGR01469 uroporphyrinogen-III C-methyltransferase
18 253 InterPro IPR006366 Uroporphyrin-III C-methyltransferase
23 251 CDD cd11642 SUMT
23 251 InterPro IPR006366 Uroporphyrin-III C-methyltransferase
11 133 Gene3D G3DSA:3.40.1010.10 -
11 133 InterPro IPR014777 Tetrapyrrole methylase, subdomain 1

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

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Structural evidence

2 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 2YBO
X-ray 2.00 Å A
100.0% 1-279
PDBe RCSB PDBj File
Viewing
PDB 2YBQ
X-ray 2.00 Å A
100.0% 1-279
PDBe RCSB PDBj File
Loaded
AlphaFold PA0510
AlphaFold — — full sequence — Loaded
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
3 0.824
2 0.514
1 0.385

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 18.23 0.818
2 2.48 0.068

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.

4 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
UP2
2YBQ 2.00 Å Open crystal
836.8 Da LogP 2.25 TPSA 361.6 2 viol. ✓ Clean C1c2c(c(c([nH]2)Cc3c(c(c([nH]3)Cc4c(c(c([nH]4)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.