A0A653M9I9 · A0A653M9I9_9MICC

  • 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.

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 site68-71substrate
Active site69Nucleophile
Site121Important for activity
Binding site131substrate
Binding site136-138substrate
Binding site142substrate
Binding site213-218NADP+ (UniProtKB | ChEBI)

GO annotations

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

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
      ARTHRO9V_100044

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Arthrobacter sp. 9V
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Arthrobacter

Accessions

  • Primary accession
    A0A653M9I9

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain30-178Glutamyl-tRNA reductase N-terminal
Domain202-323Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain338-434Tetrapyrrole 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
    461
  • Mass (Da)
    48,086
  • Last updated
    2020-04-22 v1
  • Checksum
    D8C22AFA8ACD64A9
MGITTAQYCSTGLRKSYDWGAVVLFSLVATHADIDLETVAQLSNGSSELASAALTDSSVVSGAVVLATCNRYEIYGETANGADLEAARSALVSQISELSGLNEQLVSRSFATNTGPDVTRHLFAVSAGLDSAVVGEREIAGQVRRALITAQQEGTASSGLVRLFQAASKTAKDVGAQTALGSRGLSIVSVALDLATDLAENEDWSTKKVVVFGTGAYAGATMSLLRERGCSDVSVYSSSGRAEGFVATRGGTALDADSLPAAVAAADVMIGCSGSDNRVEAADLARVRANSGKPLIAIDLALTHDFDPAVGELDGVELLTLESVRLAAPQEQAESLSQASAIVNGAATSFESEREARSVDTAIVALRRHTMNVLDAEMEKVRARHGCTAAAEEVEFALRRMVKQLLHIPTVRARELAANGQQDDYVAALEALYGIQVEQPQAAAPAAECPVDHEQIRSESA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABWLJ010000002
EMBL· GenBank· DDBJ
VXB01660.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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