{PDOC00156}
{PS51415; XYLOSE_ISOMERASE}
{BEGIN}
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* Xylose isomerase family profile *
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Xylose  isomerase  (EC 5.3.1.5) [1] is an enzyme found in microorganisms which
catalyzes  the  interconversion  of  an  aldo  sugar  D-xylose to a keto sugar
D-xylulose.  It  can  also  isomerize  D-ribose to D-ribulose and D-glucose to
D-fructose.  Xylose  isomerase  seems  to  require magnesium for its activity,
while cobalt is necessary to stabilize the tetrameric structure of the enzyme.

Xylose  isomerase  also  exists in plants [2] where it is manganese-dependent.
The enzyme has also been found in anaerobic fungi [3].

A number of residues are conserved in all known xylose isomerases. A histidine
in  the  N-terminal section of the enzyme has been shown [4] to be involved in
the catalytic mechanism of the enzyme. Two glutamate residues, a histidine and
four  aspartate  residues  are  the  metal-binding sites that bind two ions of
magnesium, cobalt, or manganese [5-7].

Three-dimensional  structures  of  xylose  isomerases show a that each subunit
contains  a  common  alpha/beta-barrel fold (see <PDB:2GLK; A>) [7] similar to
that  of  other  divalent metal-dependent TIM barrel enzymes, such as rhamnose
isomerase  [8]  and  endonuclease  4 (see <PDOC00599>) [1,5,6]. The C-terminal
smaller  part  forms  an  extended helical fold that seems to be implicated in
multimerization.

We have developed a profile that covers the entire xylose isomerase structure.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Jenkins J.; jenkins@frira.afrc.ac.uk

-Last update: February 2009 / Text revised; profile added; patterns deleted.

[ 1] Dauter Z., Dauter M., Hemker J., Witzel H., Wilson K.S.
     "Crystallisation and preliminary analysis of glucose isomerase from
     Streptomyces albus."
     FEBS Lett. 247:1-8(1989).
     PubMed=2651156
[ 2] Kristo P.A., Saarelainen R., Fagerstrom R., Aho S., Korhola M.
     "Protein purification, and cloning and characterization of the cDNA
     and gene for xylose isomerase of barley."
     Eur. J. Biochem. 237:240-246(1996).
     PubMed=8620879
[ 3] Harhangi H.R., Akhmanova A.S., Emmens R., van der Drift C.,
     de Laat W.T., van Dijken J.P., Jetten M.S., Pronk J.T.,
     Op den Camp H.J.
     "Xylose metabolism in the anaerobic fungus Piromyces sp. strain E2
     follows the bacterial pathway."
     Arch. Microbiol. 180:134-141(2003).
     PubMed=12811467; DOI=10.1007/s00203-003-0565-0
[ 4] Vangrysperre W., Ampe C., Kersters-Hilderson H., Tempst P.
     "Single active-site histidine in D-xylose isomerase from Streptomyces
     violaceoruber. Identification by chemical derivatization and peptide
     mapping."
     Biochem. J. 263:195-199(1989).
     PubMed=2604694
[ 5] Henrick K., Collyer C.A., Blow D.M.
     "Structures of D-xylose isomerase from Arthrobacter strain B3728
     containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A
     resolution, respectively."
     J. Mol. Biol. 208:129-157(1989).
     PubMed=2769749
[ 6] Chang C., Park B.C., Lee D.S., Suh S.W.
     "Crystal structures of thermostable xylose isomerases from Thermus
     caldophilus and Thermus thermophilus: possible structural determinants
     of thermostability."
     J. Mol. Biol. 288:623-634(1999).
     PubMed=10329168; DOI=10.1006/jmbi.1999.2696
[ 7] Katz A.K., Li X., Carrell H.L., Hanson B.L., Langan P., Coates L.,
     Schoenborn B.P., Glusker J.P., Bunick G.J.
     "Locating active-site hydrogen atoms in D-xylose isomerase:
     time-of-flight neutron diffraction."
     Proc. Natl. Acad. Sci. U.S.A. 103:8342-8347(2006).
     PubMed=16707576; DOI=10.1073/pnas.0602598103
[ 8] Korndoerfer I.P., Fessner W.D., Matthews B.W.
     "The structure of rhamnose isomerase from Escherichia coli and its
     relation with xylose isomerase illustrates a change between inter and
     intra-subunit complementation during evolution."
     J. Mol. Biol. 300:917-933(2000).
     PubMed=10891278; DOI=10.1006/jmbi.2000.3896

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