A0A292YYM0 · A0A292YYM0_9PSEU
- ProteinGlutamyl-tRNA reductase
- GenehemA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids469 (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: TCNR | ||||||
Active site | 48 | Nucleophile | ||||
Sequence: C | ||||||
Site | 97 | Important for activity | ||||
Sequence: H | ||||||
Binding site | 107 | substrate | ||||
Sequence: S | ||||||
Binding site | 112-114 | substrate | ||||
Sequence: ESQ | ||||||
Binding site | 118 | substrate | ||||
Sequence: Q | ||||||
Binding site | 191-196 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAMG |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia
Accessions
- Primary accessionA0A292YYM0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-154 | Glutamyl-tRNA reductase N-terminal | ||||
Sequence: VGMSHRTAPVALLEEATVGPDDVPKLLDEMLRAEHVSEVVLLTTCNRIEIYAVVDAFHGGLTDVSGVLARHSGLPLTDLTDHLYVHYAASAVQHLFSVSAGLDSMVVGESQILGQLRSAYAVADETGSVGRVLHELSQQALRVGKRVHAST | ||||||
Domain | 180-310 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: GDLHGTKAVVVGAGAMGALAAAHLRRAGAGEVVVLNRSVDRAERLAAKTSEAGTPARAGTLDLLPVELADADVLVTCTGSVGIVVGREPVAAARATTGAPLVVCDLGLPRDVDPAVVDVPGVTVVDLETLQ | ||||||
Domain | 328-426 | Tetrapyrrole biosynthesis glutamyl-tRNA reductase dimerisation | ||||
Sequence: ARTIVADEAQSYLASQRSAEVTPTVTALRRRASEVVDAELLRLDSRLPDIDPAVRDEFVRSVRRVVDKLLHTPTVQVKRLAEGPDGDSYAQALRLLFEL |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)49,000
- Last updated2017-12-20 v1
- Checksum58852A0957A95BFE