A1RQP7 · HEM1_PYRIL
- ProteinGlutamyl-tRNA reductase
- GenehemA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Miscellaneous
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Catalytic activity
- (S)-4-amino-5-oxopentanoate + NADP+ + tRNA(Glu) = H+ + L-glutamyl-tRNA(Glu) + NADPH
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47-50 | substrate | ||||
Sequence: TCGR | ||||||
Active site | 48 | Nucleophile | ||||
Sequence: C | ||||||
Site | 88 | Important for activity | ||||
Sequence: H | ||||||
Binding site | 98 | substrate | ||||
Sequence: S | ||||||
Binding site | 103-105 | substrate | ||||
Sequence: ETD | ||||||
Binding site | 109 | substrate | ||||
Sequence: Q | ||||||
Binding site | 177-182 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAVG |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glutamyl-tRNA reductase activity | |
Molecular Function | NADP binding | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamyl-tRNA reductase
- EC number
- Short namesGluTR
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionA1RQP7
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000004679 | 1-393 | Glutamyl-tRNA reductase | |||
Sequence: MDLLSPLSAIVLTYREVDTDTLGKIGEEMRKCLEQMGRGTPIYVLHTCGRVEAYLYGASPEEVQTVAETYRKYVNSVRIIAGVEAARHLFRVAAGLDSMLIGETDVLGQLEEAFDRQVRAGYTRGLLKTIVERAVRVGKRVRTETAISRGPRGLGSLSIIYVSRLLDMRQAKVAVLGAGAVGAGLAMELAARGVKKLYILNRTLEKAKEVAAKTGGEARPLTKEEVERCLRECDVVFSSVHSMEYIIDKIPEGASVKVVVDLGVPQTVASGLPVKVVRIEDLREIAEQYNAERASEIAKAEAIVEEELAILPKLLARRYIEETVSTFIETAMLAAEEEGARAGCNTATLAARTTVKRILLPLVERLKKMAEDGQIEEAVKLAQMLSQTIGRKI |
Interaction
Structure
Family & Domains
Domain
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence similarities
Belongs to the glutamyl-tRNA reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,011
- Last updated2007-02-06 v1
- ChecksumD5B0DC67046AF16A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000504 EMBL· GenBank· DDBJ | ABL87279.1 EMBL· GenBank· DDBJ | Genomic DNA |