A0A4U0ZN13 · A0A4U0ZN13_9BACT

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 site51-54substrate
Active site52Nucleophile
Site100Important for activity
Binding site110substrate
Binding site115-117substrate
Binding site121substrate
Binding site190-195NADP+ (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
      FCL48_20375

Organism names

  • Taxonomic identifier
  • Strain
    • IMCC35007
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfocapsaceae > Desulforhopalus

Accessions

  • Primary accession
    A0A4U0ZN13

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-157Glutamyl-tRNA reductase N-terminal
Domain172-307Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain321-422Tetrapyrrole 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
    424
  • Mass (Da)
    47,234
  • Last updated
    2019-07-31 v1
  • Checksum
    31C56D76DF2746B8
MPAERLLLLGVNHKTTPVEVREKIALSSGYDEPLTALKRVRGLKEYYLLSTCNRVEFLLVAQPDKNIEQEIIRFLFGEGALLQDVGKYLYILEGQAAVKHLFMVAASLDSMIVGEAQILGQLKVAYRHASQLGCTGPLLNKLLHKSFSVAKRVRTETAIGSSAVSISFAAVQLAKKIFGNLKEKNVLLVGAGEMAELAAEHLVGQGVGGVVVANRTLSRAVSLAQRFNGKAVSMDELIVQLETVDIIISSTGAKDIILYKEDVKSIMRSRMNKPLFFIDIAVPRDLDPKLNELDNVYLYDIDDLSTVVEMNRSERDKEAVKATRIVEEEALKFERYYQGLAITPAILELRQKIDSIGQYELEKTMHKLPGLTEEEKKHLEKMISAINAKVLHHPLMYLKADSCMGRDNRDKKVAIIRELFGLGD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SWCN01000024
EMBL· GenBank· DDBJ
TKB06628.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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