Protein profile

PA1276

threonine-phosphate decarboxylase

Genome: NC_002516.2

Gene: cobC PA1276 Structure source: AlphaFold UniProt Q9I468
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Amino acids 331
Annotations 7
Features 15
PDB binders 6
Druggability 0.881

Overview

Basic information about this protein and its source genome.

Accession
PA1276
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
cobC PA1276
Status
annotated
Amino acids
331
Structure source
AlphaFold
EC
4.1.1.81
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0048472 Catalysis of the reaction: O-phospho-L-threonine + H+ = (R)-1-aminopropan-2-yl phosphate + CO2. 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: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:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

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 0.881
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0048472 Catalysis of the reaction: O-phospho-L-threonine + H+ = (R)-1-aminopropan-2-yl phosphate + CO2.
  • 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: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:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
4 322 NCBIfam TIGR01140 threonine-phosphate decarboxylase CobD
4 322 InterPro IPR005860 L-threonine-O-3-phosphate decarboxylase
231 261 Coils Coil Coil
23 300 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
23 300 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
34 237 Gene3D G3DSA:3.40.640.10 -
34 237 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
54 308 Pfam PF00155 Aminotransferase class I and II
54 308 InterPro IPR004839 Aminotransferase, class I/classII
23 231 CDD cd00609 AAT_like
189 202 ProSitePatterns PS00105 Aminotransferases class-I pyridoxal-phosphate attachment site.
189 202 InterPro IPR004838 Aminotransferases, class-I, pyridoxal-phosphate-binding site
51 301 PANTHER PTHR42885 HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED
12 313 SUPERFAMILY SSF53383 PLP-dependent transferases
12 313 InterPro IPR015424 Pyridoxal phosphate-dependent transferase

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 PA1276
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
4 0.881
1 0.383

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.

56 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
33P
1LC8
P97084 386.2 Da LogP 0.29 TPSA 178.7 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC[C@@H](C)OP(=O)(O)O…
HSA
1FG3
P06986 221.2 Da LogP -0.61 TPSA 121.5 ✓ Ro5 ✓ Clean c1c(nc[nH]1)CC(COP(=O)(O)O)N
PMP
1FG7
P06986 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
SIN
4R5Z
P9WML5 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
TLA
3P1T
Q63U92 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)O)O
TPO
1LC7
P97084 199.1 Da LogP -1.10 TPSA 130.1 ✓ Ro5 ✓ Clean C[C@H]([C@@H](C(=O)O)N)OP(=O)(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.