Domain

Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase (IPR006151)

Short name: Shikm_DH/Glu-tRNA_Rdtase

Domain relationships

  • NAD(P)-binding domain (IPR016040)
    • Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase (IPR006151)

Description

This entry represents a domain found in shikimate and quinate dehydrogenases, as well as glutamyl-tRNA reductases.

Shikimate 5-dehydrogenase (EC:1.1.1.25) catalyses the conversion of shikimate to 5-dehydroshikimate [PMID: 12906831, PMID: 12837789]. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids [PMID: 15012217]. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites, 3-dehydroquinate and dehydroshikimate.

Glutamyl-tRNA reductase (EC:1.2.1.70) catalyzes the first step of tetrapyrrole biosynthesis in plants, archaea and most bacteria. The dimeric enzyme has an unusual V-shaped architecture where each monomer consists of three domains linked by a long 'spinal' alpha-helix. The central catalytic domain specifically recognises the glutamate moiety of the substrate [PMID: 16228559].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam