Protein profile

PA0430

5,10-methylenetetrahydrofolate reductase

Genome: NC_002516.2

Gene: PA0430 metF Structure source: AlphaFold UniProt Q9I687
Export view
Amino acids 290
Annotations 8
Features 11
PDB binders 2
Druggability 0.656

Overview

Basic information about this protein and its source genome.

Accession
PA0430
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0430 metF
Status
annotated
Amino acids
290
Structure source
AlphaFold
EC
1.5.1.54
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0106312 Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD+ = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADH + H+. GO:0004489 Catalysis of the reaction: 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+. GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.593
Human E-value
5.369999999999999e-23
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 0.656
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MVASKEPIMSQSERRFSFEFFPAKTEAGHEKLLATARNLAGYKPDFFSCTYGAGGSTRDRTLSTVLQLDGEVKVPTAPHLSCVGDSKAELRELLGRYREAGIRRIVALRGDLPSGMGMASGELRYANELVDFIRTETGDHFHIEVAAYPEVHPQARSFEDDLANFVRKVKAGASSAITQYFFNADAYFYFVERVAKLGVDIPVVPGIMPITNYSKLARFSDACGAELPRWIRKQLEAYGDDSRSIQAFGEQVISEMCERLLEGGAPGLHFYTLNQADPSLAIWKNLQLPR

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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • GO:0106312 Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD+ = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADH + H+.
  • GO:0004489 Catalysis of the reaction: 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+.
  • GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
  • GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.
  • GO:0006555 The chemical reactions and pathways involving L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
10 286 Pfam PF02219 Methylenetetrahydrofolate reductase
10 286 InterPro IPR003171 Methylenetetrahydrofolate reductase-like
16 286 CDD cd00537 MTHFR
16 286 InterPro IPR003171 Methylenetetrahydrofolate reductase-like
5 289 Gene3D G3DSA:3.20.20.220 -
8 288 SUPERFAMILY SSF51730 FAD-linked oxidoreductase
8 288 InterPro IPR029041 FAD-linked oxidoreductase-like
16 287 NCBIfam TIGR00676 methylenetetrahydrofolate reductase [NAD(P)H]
16 287 InterPro IPR004620 5,10-methylenetetrahydrofolate reductase
9 288 PANTHER PTHR45754 METHYLENETETRAHYDROFOLATE REDUCTASE
9 289 FunFam G3DSA:3.20.20.220:FF:000014 Methylenetetrahydrofolate reductase

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

Loading 3D structure...

Legend High Medium Low

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 PA0430
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 0.656
1 0.42
3 0.232

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.

52 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
4HF
2FMN
P0AEZ1 449.5 Da LogP 0.68 TPSA 187.5 1 viol. ✓ Clean c1cc(sc1CC[C@@H]2CC3=C(NC2)N=C(NC3=O)N)C(=O)N[C…
C2F
1ZP4
P0AEZ1 459.5 Da LogP -0.26 TPSA 202.8 1 viol. ✓ Clean C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)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.