A0A0U5AVP8 · A0A0U5AVP8_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.

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 site53-56substrate
Active site54Nucleophile
Site105Important for activity
Binding site115substrate
Binding site120-122substrate
Binding site126substrate
Binding site195-200NADP+ (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
      THC_0968

Organism names

  • Taxonomic identifier
  • Strain
    • TF1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Thermodesulfobacteria > Thermodesulfobacteriales > Thermodesulfobacteriaceae > Caldimicrobium

Accessions

  • Primary accession
    A0A0U5AVP8

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-162Glutamyl-tRNA reductase N-terminal
Domain177-312Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain326-424Tetrapyrrole 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
    457
  • Mass (Da)
    51,889
  • Last updated
    2016-03-16 v1
  • MD5 Checksum
    EEAFAF78D475DEEE2816F77E7F1DD96E
MVTNFKLCLIGVNHKTTPVEIREKLSFTSAHIHPLEKFQKFSTSFKEAFFLSTCNRVEFFFVHHPDQRPLLLEAFSNFLKEETGFTLENLEPHFYFLEDENAIRHLFEVACGLDSLVLGEPQILGQLKEAYRVALHYKTSGLILNKLMHRAFFVAKRVRTETGIGGGAVSVSYAASQLAKKVLGSLRDKKVLLIGAGEMAELACQHLLTLGATEILIANRTLSKAIELAERFKGKASSLEELPEVLLQADIVISSTGAPGFIITKKLLSPLLKPRKFKPLFIIDIAVPRDVEPAVNELENVYLFDIDDLKEVVEENLKARKNEALRAKTIIEEEVHKVKKWLSELAINPTLRRLTEKAETLRQKELEKTLKKLRNISPEDKEALEILTKSLVQKLLSYPIHFLKRGYHEEGKFAISLIREIYQLDEGEESAKKELFLEDTLEEASLQKEDSSVKILQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP014945
EMBL· GenBank· DDBJ
BAU23352.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
Help