A0A292YYM0 · A0A292YYM0_9PSEU

  • Protein
    Glutamyl-tRNA reductase
  • Gene
    hemA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site47-50substrate
Active site48Nucleophile
Site97Important for activity
Binding site107substrate
Binding site112-114substrate
Binding site118substrate
Binding site191-196NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionglutamyl-tRNA reductase activity
Molecular FunctionNADP binding
Biological Processprotoporphyrinogen IX biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamyl-tRNA reductase
  • EC number
  • Short names
    GluTR

Gene names

    • Name
      hemA
    • ORF names
      TOK_2892

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • N23
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia

Accessions

  • Primary accession
    A0A292YYM0

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-154Glutamyl-tRNA reductase N-terminal
Domain180-310Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain328-426Tetrapyrrole biosynthesis glutamyl-tRNA reductase dimerisation

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 status
    Complete
  • Length
    469
  • Mass (Da)
    49,000
  • Last updated
    2017-12-20 v1
  • Checksum
    58852A0957A95BFE
MLVVGMSHRTAPVALLEEATVGPDDVPKLLDEMLRAEHVSEVVLLTTCNRIEIYAVVDAFHGGLTDVSGVLARHSGLPLTDLTDHLYVHYAASAVQHLFSVSAGLDSMVVGESQILGQLRSAYAVADETGSVGRVLHELSQQALRVGKRVHASTGIDAAGASVVSEALADASRSLGREPGDLHGTKAVVVGAGAMGALAAAHLRRAGAGEVVVLNRSVDRAERLAAKTSEAGTPARAGTLDLLPVELADADVLVTCTGSVGIVVGREPVAAARATTGAPLVVCDLGLPRDVDPAVVDVPGVTVVDLETLQRRLTDRVDTADADVVAAARTIVADEAQSYLASQRSAEVTPTVTALRRRASEVVDAELLRLDSRLPDIDPAVRDEFVRSVRRVVDKLLHTPTVQVKRLAEGPDGDSYAQALRLLFELDPQTTAAVATPGVTGTSARPGDDVVAALGVELREPRADEEATR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BEGX01000029
EMBL· GenBank· DDBJ
GAY08936.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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