The domain within your query sequence starts at position 124 and ends at position 227; the E-value for the Shikimate_DH domain shown below is 7.1e-11.

AIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQGD
VRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGA

Shikimate_DH

• PFAM accession number: PF01488
• Interpro abstract (IPR006151):

  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 [ (PUBMED:12906831) (PUBMED:12837789) ]. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids [ (PUBMED: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 [ (PUBMED:16228559) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Shikimate_DH