C3L6Z7 · HEM1_BACAC

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
    • Ordered locus names
      BAMEG_4733

Organism names

Accessions

  • Primary accession
    C3L6Z7

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001905021-444Glutamyl-tRNA reductase

Interaction

Subunit

Homodimer.

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
    444
  • Mass (Da)
    49,825
  • Last updated
    2009-06-16 v1
  • Checksum
    4BB7F3FC998B0643
MHILVVSVNYRTAPVEFREKLTFQAAELERAMTTLQNQKSVLENVIVSTCNRTEIYAVVDQLHTGRYYIKKFLADWFQLEIEEVAPYLTIFEQDGAIDHLFRVTCGLDSMVVGETQILGQIKDSFLEAQQVKATGTIFNELFKQVITLAKRAHSETTIGESAMSVSYAAVELGKKIFGELTDCHVLILGAGKMGELALQNLYGSGARKVTVMNRTLSKAEIMAEKYMGHAKPLSELQCALLEADILISSTGASDYVITKEMMTKVEKMRSGRPLFMVDIAVPRDIDPAIDELEGSFLYDIDDLQGVVEANRAERLKEAEKIQFMIEEEIVLFKTWLSTLGVVPLISALRDKALAIQSETMESLERKIPNLSDRERKVISKHTKSIINQLLKDPILVAKEIAAEEGADEKLALFAKIFDLEMEDVESRAEEVEHKRVWTPSVPSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001215
EMBL· GenBank· DDBJ
ACP15465.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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