SMART: Pfam domain SKI

The domain within your query sequence starts at position 13 and ends at position 60; the E-value for the SKI domain shown below is 2.9e-12.

SGSGKSTVGALLASKLGWKFYDADDYHSEENRIKMAKGVPLSDQRCGF

SKI

PFAM accession number:	PF01202
Interpro abstract (IPR031322):	Shikimate kinase ( EC 2.7.1.71 ) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [ (PUBMED:7612934) ]. The enzyme catalyses the following reaction: ATP + shikimate = ADP + shikimate-3-phosphate The protein is found in bacteria (gene aroK or aroL), plants and fungi (where it is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994, the 3D structure of shikimate kinase was predicted to be very close to that of adenylate kinase, suggesting a functional similarity as well as an evolutionary relationship [ (PUBMED:7703851) ]. This prediction has since been confirmed experimentally. The protein is reported to possess an alpha/beta fold, consisting of a central sheet of five parallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase [ (PUBMED:9600856) ]. The N terminus of threonine synthase-like 1 from metazoan shares protein sequence similarity with shikimate kinase and is included in this entry. However, their functions may be different.

PFAM accession number:

PF01202

Interpro abstract (IPR031322):

Shikimate kinase ( EC 2.7.1.71 ) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [ (PUBMED:7612934) ]. The enzyme catalyses the following reaction:

ATP + shikimate = ADP + shikimate-3-phosphate

The protein is found in bacteria (gene aroK or aroL), plants and fungi (where it is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994, the 3D structure of shikimate kinase was predicted to be very close to that of adenylate kinase, suggesting a functional similarity as well as an evolutionary relationship [ (PUBMED:7703851) ]. This prediction has since been confirmed experimentally. The protein is reported to possess an alpha/beta fold, consisting of a central sheet of five parallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase [ (PUBMED:9600856) ].

The N terminus of threonine synthase-like 1 from metazoan shares protein sequence similarity with shikimate kinase and is included in this entry. However, their functions may be different.

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