Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01464
- Gene
- AHE44002.1 hemA
- Status
- annotated
- Amino acids
- 418
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 92.105
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 89.61
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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: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.
- GO:0019353 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX from other compounds, including glutamate.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 2 | 161 | FunFam | G3DSA:3.30.460.30:FF:000001 | Glutamyl-tRNA reductase |
| 172 | 306 | Pfam | PF01488 | Shikimate / quinate 5-dehydrogenase |
| 172 | 306 | InterPro | IPR006151 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase |
| 99 | 122 | ProSitePatterns | PS00747 | Glutamyl-tRNA reductase signature. |
| 99 | 122 | InterPro | IPR018214 | Glutamyl-tRNA reductase, conserved site |
| 6 | 156 | Pfam | PF05201 | Glutamyl-tRNAGlu reductase, N-terminal domain |
| 6 | 156 | InterPro | IPR015895 | Glutamyl-tRNA reductase, N-terminal |
| 3 | 318 | CDD | cd05213 | NAD_bind_Glutamyl_tRNA_reduct |
| 161 | 312 | Gene3D | G3DSA:3.40.50.720 | - |
| 338 | 358 | Coils | Coil | Coil |
| 4 | 418 | NCBIfam | TIGR01035 | glutamyl-tRNA reductase |
| 4 | 418 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 1 | 158 | SUPERFAMILY | SSF69742 | Glutamyl tRNA-reductase catalytic, N-terminal domain |
| 1 | 158 | InterPro | IPR036343 | Glutamyl-tRNA reductase, N-terminal domain superfamily |
| 2 | 418 | Hamap | MF_00087 | Glutamyl-tRNA reductase [hemA]. |
| 2 | 418 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 320 | 415 | Pfam | PF00745 | Glutamyl-tRNAGlu reductase, dimerisation domain |
| 320 | 415 | InterPro | IPR015896 | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain |
| 161 | 313 | FunFam | G3DSA:3.40.50.720:FF:000031 | Glutamyl-tRNA reductase |
| 1 | 417 | PANTHER | PTHR43013 | GLUTAMYL-TRNA REDUCTASE |
| 2 | 160 | Gene3D | G3DSA:3.30.460.30 | - |
| 2 | 160 | InterPro | IPR036343 | Glutamyl-tRNA reductase, N-terminal domain superfamily |
| 317 | 417 | SUPERFAMILY | SSF69075 | Glutamyl tRNA-reductase dimerization domain |
| 317 | 417 | InterPro | IPR036453 | Glutamyl tRNA-reductase dimerization domain superfamily |
| 1 | 418 | PIRSF | PIRSF000445 | GluTR |
| 1 | 418 | InterPro | IPR000343 | Glutamyl-tRNA reductase |
| 162 | 315 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 162 | 315 | InterPro | IPR036291 | NAD(P)-binding 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 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GUC0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01464
|
ColabFold | — | — | 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 |
|---|---|---|---|---|---|---|---|
| 8 | 0.515 | ||||||
| 31 | 0.024 | ||||||
| 3 | 0.019 | ||||||
| 24 | 0.018 |
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 | 8.09 | 0.364 | ||||||
| 2 | 3.86 | 0.122 | ||||||
| 3 | 2.35 | 0.05 | ||||||
| 4 | 1.32 | 0.012 |
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 |
|---|---|---|---|---|---|---|---|
| 11 | 0.516 |
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 | 2.29 | 0.058 | ||||||
| 2 | 1.46 | 0.02 |