O69108 · HEM1_PAEMA

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
Site99Important for activity
Binding site109substrate
Binding site114-116substrate
Binding site120substrate
Binding site189-194NADP+ (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

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 8244 / DSM 24 / IAM 1227 / JCM 2500 / NBRC 15307 / NCIMB 9368 / NCTC 6355 / NRRL B-394 / VKM B-506
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus

Accessions

  • Primary accession
    O69108

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001140501-437Glutamyl-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    49,394
  • Last updated
    1998-08-01 v1
  • Checksum
    51EAD60077424FB2
MHIVVVGLNYRTAPVEVRERFSFAEKDMPQALQELLRTKSVLEGVIIATCNRTEIYVVVDRLHMCGYFIRSFMERWFGVPREEFTRHLYMYEDEQAVRHLFRVACGLDSMVLGETQILGQVKSAFLLSQRQKGTGTWFNMLFKQAVTLGKRAHSETAIGQSAVSISYAAVELGKRIFGSFSGKRVLILGAGKMSELTAKHLSGGGADEVIVANRTYARAQELAAKFDGTPCTMQEAMERLADVDILISSTGAEGIRDHVGQVERSMKRRPDRPLFMIDIAVPRDIEPEIGVLENVFLYDIDDLEGIVENNLEMRRAEAVKIDKMIEEEMQVFANWLQTLGVKPVIRALQEKAAHIHESTLDSMFNKLPELDERQRKVIRRLTKSILNQMMHDPINRIKEMAGGKQGAEALEMFTQIFALEKHLEAGAPVGRGKRRLP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF064061
EMBL· GenBank· DDBJ
AAC18585.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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