Overview
Basic information about this protein and its source genome.
- Accession
- PA4666
- Gene
- PA4666 hemA
- Status
- annotated
- Amino acids
- 422
- Structure source
- AlphaFold
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
4- GO:0008883 Catalysis of the reaction: (S)-4-amino-5-oxopentanoate + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + H+ + NADPH.
- GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
- GO:0019353 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX from other compounds, including glutamate.
- GO:0033014 The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 4 | 415 | NCBIfam | TIGR01035 | glutamyl-tRNA reductase |
| 4 | 415 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 170 | 304 | Pfam | PF01488 | Shikimate / quinate 5-dehydrogenase |
| 170 | 304 | InterPro | IPR006151 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase |
| 315 | 416 | SUPERFAMILY | SSF69075 | Glutamyl tRNA-reductase dimerization domain |
| 315 | 416 | InterPro | IPR036453 | Glutamyl tRNA-reductase dimerization domain superfamily |
| 3 | 316 | CDD | cd05213 | NAD_bind_Glutamyl_tRNA_reduct |
| 2 | 159 | FunFam | G3DSA:3.30.460.30:FF:000001 | Glutamyl-tRNA reductase |
| 160 | 311 | Gene3D | G3DSA:3.40.50.720 | - |
| 6 | 154 | Pfam | PF05201 | Glutamyl-tRNAGlu reductase, N-terminal domain |
| 6 | 154 | InterPro | IPR015895 | Glutamyl-tRNA reductase, N-terminal |
| 1 | 422 | PIRSF | PIRSF000445 | GluTR |
| 1 | 422 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 160 | 313 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 160 | 313 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 2 | 416 | Hamap | MF_00087 | Glutamyl-tRNA reductase [hemA]. |
| 2 | 416 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 97 | 120 | ProSitePatterns | PS00747 | Glutamyl-tRNA reductase signature. |
| 97 | 120 | InterPro | IPR018214 | Glutamyl-tRNA reductase, conserved site |
| 159 | 311 | FunFam | G3DSA:3.40.50.720:FF:000031 | Glutamyl-tRNA reductase |
| 319 | 415 | Pfam | PF00745 | Glutamyl-tRNAGlu reductase, dimerisation domain |
| 319 | 415 | InterPro | IPR015896 | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain |
| 2 | 158 | Gene3D | G3DSA:3.30.460.30 | - |
| 2 | 158 | InterPro | IPR036343 | Glutamyl-tRNA reductase, N-terminal domain superfamily |
| 1 | 417 | PANTHER | PTHR43013 | GLUTAMYL-TRNA REDUCTASE |
| 1 | 156 | SUPERFAMILY | SSF69742 | Glutamyl tRNA-reductase catalytic, N-terminal domain |
| 1 | 156 | InterPro | IPR036343 | Glutamyl-tRNA reductase, N-terminal domain superfamily |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA4666
|
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 |
|---|---|---|---|---|---|---|---|
| 8 | 0.576 | ||||||
| 2 | 0.522 | ||||||
| 9 | 0.319 |