A0A6I2F7S2 · A0A6I2F7S2_9MICO

  • 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.

Type
IDPosition(s)Description
Binding site46-49substrate
Active site47Nucleophile
Site101Important for activity
Binding site111substrate
Binding site116-118substrate
Binding site122substrate
Binding site191-196NADP+ (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
      GE115_08145

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CFH 90414
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Agromyces

Accessions

  • Primary accession
    A0A6I2F7S2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain6-158Glutamyl-tRNA reductase N-terminal
Domain173-322Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain336-427Tetrapyrrole biosynthesis glutamyl-tRNA reductase dimerisation
Region433-467Disordered

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
    467
  • Mass (Da)
    49,067
  • Last updated
    2020-08-12 v1
  • Checksum
    81360AECD82B6010
MLICLTASHKNAGFDLLERLSATADDAGRRMVAGHEAVQGAVVVATCNRFEAYLDLDAPEGDSPVDAVHGAIRSVGEVSGLEADELRTTFGFAHGNAVAAHLFAVASGLESVVVGEGEIAGQVRRSLERARSEGTTTPELERLFQRASQTSRKVKNRTGIGAEGRSLVRLSLELAESRITDWAQTKVLLVGTGRYAGASLAALRDRGVVDVSVHSPSGRGAKFAASHELPAVPGESFARAVAEADVIVACTLAEVFVVDRALIAAGREQLALDRAPVRTLDGAIVPVADRRQLIIDLGLPRNVDPGVVEVTGVELLDLETIKIHAPMEEFAATDAARDLVQRAARNFGDVAEELDLAPTVVALRKHVFDVLDAEIERSRAHDDDGRIESALRHMAGVLLHTPMVRSREHARAGEQRAFIDAVEALFGVTATDASSSVSGSSSAAGSSSAPDSSSASGTSSVSDSRAV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WJIF01000003
EMBL· GenBank· DDBJ
MRG59837.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp