Protein profile

PA1252

bifunctional Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2- carboxylate reductase

Genome: NC_002516.2

Gene: lhpH lhpD PA1252 Structure source: AlphaFold UniProt Q9I492
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Amino acids 334
Annotations 10
Features 11
PDB binders 2
Druggability 0.503

Overview

Basic information about this protein and its source genome.

Accession
PA1252
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
lhpH lhpD PA1252
Status
annotated
Amino acids
334
Structure source
AlphaFold
EC
1.5.1.21 1.5.1.-
GO
GO:0047125 Catalysis of the reaction: NADP+ + L-pipecolate = NADPH + delta1-piperideine-2-carboxylate. GO:0042802 Binding to an identical protein or proteins. GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0042803 Binding to an identical protein to form a homodimer. GO:0050241 Catalysis of the reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+. GO:0006560 The chemical reactions and pathways involving proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

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 0.503
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 8 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

8
  • GO:0047125 Catalysis of the reaction: NADP+ + L-pipecolate = NADPH + delta1-piperideine-2-carboxylate.
  • GO:0042802 Binding to an identical protein or proteins.
  • GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
  • GO:0042803 Binding to an identical protein to form a homodimer.
  • GO:0050241 Catalysis of the reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+.
  • GO:0006560 The chemical reactions and pathways involving proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
  • GO:0019470 The chemical reactions and pathways resulting in the breakdown of trans-4-hydroxy-L-proline.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
5 329 Pfam PF02615 Malate/L-lactate dehydrogenase
5 329 InterPro IPR003767 Malate/L-lactate dehydrogenase-like
68 303 FunFam G3DSA:3.30.1370.60:FF:000002 Malate/L-lactate family dehydrogenase
68 303 Gene3D G3DSA:3.30.1370.60 Hypothetical oxidoreductase yiak; domain 2
68 303 InterPro IPR043143 Malate/L-sulfolactate/L-lactate dehydrogenase-like, NADPH binding domain
13 332 Gene3D G3DSA:1.10.1530.10 -
13 332 InterPro IPR043144 Malate/L-sulfolactate/L-lactate dehydrogenase-like, alpha-helical domain
1 333 SUPERFAMILY SSF89733 L-sulfolactate dehydrogenase-like
1 333 InterPro IPR036111 Malate/L-sulfolactate/L-lactate dehydrogenase-like superfamily
3 332 PANTHER PTHR11091 OXIDOREDUCTASE-RELATED
3 332 InterPro IPR003767 Malate/L-lactate dehydrogenase-like

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 PA1252
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
2 0.503

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.

20 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
PYC
2CWH
Q4U331 110.1 Da LogP -0.62 TPSA 55.9 ✓ Ro5 ✓ Clean c1cc([nH]c1)C(=O)[O-]
TLA
1S20
P37672 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=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.