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The annotation and conditions in this rule are derived from the following entries: P0A6X1 (HEM1_ECOLI), Q9UXR8 (HEM1_METKA), P28462 (HEM1_CHLP8), P42809 (HEM1_METTM), P28463 (HEM1_SYNY3), Q59292 (HEMA_CLOJO), P42808 (HEM1_XANCH)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00087
    • gene location = Plastid
    • fragment ≠ the sequence is fragmented

Special conditions

    • gene location = Plastid; Chloroplast
    • proteome property = PHOTOSYN=Yes
    • Subsequence at position 47 - 50 aligns to "T-C-x-R" in entry Q9UXR8 (individually applies "Substrate binding")
    • Subsequence at position 48 - 48 aligns to "C" in entry Q9UXR8 (individually applies "Nucleophile")
    • Subsequence at position 84 - 84 aligns to "H" in entry Q9UXR8 (individually applies "Important for activity")
    • Subsequence at position 94 - 94 aligns to "S" in entry Q9UXR8 (individually applies "Substrate")
    • Subsequence at position 99 - 101 aligns to "[ED]-x-[EDQ]" in entry Q9UXR8 (individually applies "Substrate binding")
    • Subsequence at position 105 - 105 aligns to "Q" in entry Q9UXR8 (individually applies "Substrate")
    • Subsequence at position 174 - 179 aligns to entry Q9UXR8 (individually applies "NADP")

... then these annotations are applied i

Protein namei

  • Recommended name:
    Glutamyl-tRNA reductase (EC:1.2.1.70)
    Short name:
    GluTR

Gene namei

  • Name:hemA

Functioni

  • Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).

Domaini

  • 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.

Miscellaneousi

  • 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.

Subunit structurei

  • Homodimer.

Pathwayi

  • Pathwayi: protoporphyrin-IX biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu). This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.
  • Pathwayi: chlorophyll biosynthesis

    This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

Catalytic activityi

  • L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

Sequence similaritiesi

Subcellular locationi

Nucleotide bindingi

  • NADP (to residues corresponding to positions 174 - 179)

Sitei

  • Important for activity (to residues corresponding to position 84)

Active sitei

  • Nucleophile (to residues corresponding to position 48)

Regioni

  • Substrate binding (to residues corresponding to positions 47 - 50)
  • Substrate binding (to residues corresponding to positions 99 - 101)

Binding sitei

  • Substrate (to residues corresponding to position 94)
  • Substrate (to residues corresponding to position 105)

Keywordsi

GO (Gene Ontology) termsi