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Q88PW6 · HEM1_PSEPK

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 site49-52substrate
Active site50Nucleophile
Site97Important for activity
Binding site107substrate
Binding site112-114substrate
Binding site118substrate
Binding site187-192NADP+ (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
      PP_0732

Organism names

Accessions

  • Primary accession
    Q88PW6

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001140591-425Glutamyl-tRNA reductase

Proteomic databases

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
    425
  • Mass (Da)
    46,306
  • Last updated
    2003-06-01 v1
  • MD5 Checksum
    3FCF81F77F4FE860671CE10FB771CC28
MAFLALGINHKTASVDVRERVAFTPEQLVDALQQLCRLTSSREAAILSTCNRSELYIEQDHLSADAVLQWLADYHRLSIDELRASAYVHEEHDAVKHMMRVASGLDSLVLGEPQILGQMKSAYAVAREAGTVGPLLGRLFQATFSAAKQVRTDTAIGENPVSVAFAAVSLAKQIFADLGRSQALLIGAGETITLVARHLHEQGVRRIVVANRTLERASILAEQFGAHAVLLADIPQELANSDIVISSTASQLPILGKGAVESALKQRRHKPIFMVDIAVPRDIETEVGELDDVYLYTVDDLHDVVAENLKSRQGAAQAAEELVSVGAEDFMLRLRELAAVDVLRAYRQQSERLRDEELQKALRLLANGGNPEDVLAQLARGLTNKLLHAPSVQLKKLSAEGRLDALAMAQELFALNEGSTDKSPQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE015451
EMBL· GenBank· DDBJ
AAN66357.1
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.
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