A1RQP7 · HEM1_PYRIL

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 site47-50substrate
Active site48Nucleophile
Site88Important for activity
Binding site98substrate
Binding site103-105substrate
Binding site109substrate
Binding site177-182NADP+ (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
    • Ordered locus names
      Pisl_0096

Organism names

Accessions

  • Primary accession
    A1RQP7

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000046791-393Glutamyl-tRNA reductase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

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
    393
  • Mass (Da)
    43,011
  • Last updated
    2007-02-06 v1
  • Checksum
    D5B0DC67046AF16A
MDLLSPLSAIVLTYREVDTDTLGKIGEEMRKCLEQMGRGTPIYVLHTCGRVEAYLYGASPEEVQTVAETYRKYVNSVRIIAGVEAARHLFRVAAGLDSMLIGETDVLGQLEEAFDRQVRAGYTRGLLKTIVERAVRVGKRVRTETAISRGPRGLGSLSIIYVSRLLDMRQAKVAVLGAGAVGAGLAMELAARGVKKLYILNRTLEKAKEVAAKTGGEARPLTKEEVERCLRECDVVFSSVHSMEYIIDKIPEGASVKVVVDLGVPQTVASGLPVKVVRIEDLREIAEQYNAERASEIAKAEAIVEEELAILPKLLARRYIEETVSTFIETAMLAAEEEGARAGCNTATLAARTTVKRILLPLVERLKKMAEDGQIEEAVKLAQMLSQTIGRKI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000504
EMBL· GenBank· DDBJ
ABL87279.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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