Q48MV5 · HEM1_PSE14

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
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

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
      PSPPH_0996

Organism names

Accessions

  • Primary accession
    Q48MV5

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000046681-425Glutamyl-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
    425
  • Mass (Da)
    46,121
  • Last updated
    2005-09-13 v1
  • Checksum
    3519BB73F5501AD1
MAFLALGINHKTASVDVRERVAFTPEQLVEALQQLCHLTESREAAILSTCNRSELYIEHEHLGADSILAWLANYHHLSLEELRASAYVHEDDAAVRHMMRVASGLDSLVLGEPQILGQMKSAYAVAREAGTVGPLLGRLFQATFSAAKQVRTDTAIGENPVSVAFAAVSLAKQIFSDLQRSQALLIGAGETITLVARHLHDLGVKRIVVANRTLERASMLAAEFGAHAVLLSDIPAELVNSDIVISSTASQLPILGKGAVESALKLRKHKPIFMVDIAVPRDIEPEVGELDDVYLYSVDDLHEVVAENLKSRQGAALAAEQLVSVGAEDFMSRLRELAAVDVLRAYRQQSERLRDEELSKAQRMLANGSNAEDVLIQLARGLTNKLLHAPSVQLKKLSAEGRVDALAMAQELFALGEGSTDKTPQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000058
EMBL· GenBank· DDBJ
AAZ36291.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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