A0A2U8QUK2 · A0A2U8QUK2_9FLAO

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.

Type
IDPosition(s)Description
Binding site57-60substrate
Active site58Nucleophile
Site103Important for activity
Binding site113substrate
Binding site118-120substrate
Binding site124substrate
Binding site193-198NADP+ (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
      DI487_07495

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MEBiC07310
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Flavobacterium

Accessions

  • Primary accession
    A0A2U8QUK2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-160Glutamyl-tRNA reductase N-terminal
Domain181-305Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain319-413Tetrapyrrole 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    416
  • Mass (Da)
    47,083
  • Last updated
    2018-09-12 v1
  • MD5 Checksum
    C7330B3E78AEEC0422D5A73ABFC910D7
MNNSNTNKPLSFYVVGLSYKKADAEMRGKFSLDEKAKNDLLQQAKTEHIDSLVTISTCNRTEIYGFAQHPFQLIKLLCDNSQGSVEDFQRVAYVYKNREAIDHIFRVGTGLDSQILGDFEIISQIKQGFVDSKKESLANAYLERLTNAVIQASKRVKNETEISSGATSVSFAAVQYIMNNIPDIGNKRILLFGTGKIGRNTCENLVKHTKNDHIVLINRTKEKAEKIAGKFNLIVKDYADLQVEIQNADVLVVATGAQNPTVDAAILNLKKPLLILDLSIPKNVNEDVRNIDGVTLIHMDHLSQITDETLEKRKQHIPAAEKIITEVADEFAGWTKARKFAPTIHSLKEKLADIKKAELNYQRKKFENFNEEQAEIISNRIIQKITTHFANHLKDEDTMVDESIQWIEKVFRLNNN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029463
EMBL· GenBank· DDBJ
AWM13721.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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