A0AA50QB35 · A0AA50QB35_9GAMM

  • 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.

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 site49-52substrate
Active site50Nucleophile
Site98Important for activity
Binding site108substrate
Binding site113-115substrate
Binding site119substrate
Binding site188-193NADP+ (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
      PU634_11295

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NTOU-MSR1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Oceanimonas

Accessions

  • Primary accession
    A0AA50QB35

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain6-155Glutamyl-tRNA reductase N-terminal
Domain171-305Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Coiled coil208-235
Domain319-414Tetrapyrrole 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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    46,674
  • Last updated
    2024-01-24 v1
  • Checksum
    8D11881BCB724E1E
MSLLVLGINHKTASVALRERVAFGPDLAPRALQELSNTQGVAETVILSTCNRTELYCSLKDDGDSDVVRHWLQRFHNLDEDELTACLYQHQGEEAIRHLMRVACGLDSLVLGEPQILGQIKQAYSQSHQAGTLKGLLERLFQKSFSVAKRVRTETDIGASAVSVAFAAVSLAKRIFSDLGRTKVLLVGAGETVELVARHLKEQSVTRMMVANRTLERAQKLAQEFEAEVMTLEQIPEFLPQADIVISSTASPLPIIGKGMVERALKVRRHKPILLVDIAVPRDIEPEVDELNDAYLYTVDDLQGIIEQNLEARKRAAAQAERIILEERDQFMAWYRSLRSVDLIRDYRAQAESVRQQELARALQALAQGDDATLVMQQLTRRLTNKLIHTPTQALSQAGKDGDQDMLAVLSRSLGISRP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP118224
EMBL· GenBank· DDBJ
WMC09701.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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