Phosphoglucomutase (EC 188.8.131.52) (PGM). PGM is an enzyme responsible for
the conversion of D-glucose 1-phosphate into D-glucose 6-phosphate. PGM
participates in both the breakdown and synthesis of glucose .
Phosphomannomutase (EC 184.108.40.206) (PMM). PMM is an enzyme responsible for
the conversion of D-mannose 1-phosphate into D-mannose 6-phosphate. PMM is
required for different biosynthetic pathways in bacteria. For example, in
enterobacteria such as Escherichia coli there are two different genes
coding for this enzyme: rfbK which is involved in the synthesis of the O
antigen of lipopolysaccharide and cpsG which is required for the synthesis
of the M antigen capsular polysaccharide . In Pseudomonas aeruginosa PMM
(gene algC) is involved in the biosynthesis of the alginate layer  and
in Xanthomonas campestris (gene xanA) it is involved in the biosynthesis of
xanthan . In Rhizobium strain ngr234 (gene noeK) it is involved in the
biosynthesis of the nod factor.
Phosphoacetylglucosamine mutase (EC 220.127.116.11) which converts N-acetyl-D-
glucosamine 1-phosphate into the 6-phosphate isomer.
The catalytic mechanism of both PGM and PMM involves the formation of a
phosphoserine intermediate . The sequence around the serine residue is well
conserved and can be used as a signature pattern.
In addition to PGM and PMM there are at least three uncharacterized proteins
that belong to this family [5,6]:
Urease operon protein ureC from Helicobacter pylori.
Escherichia coli protein mrsA.
Paramecium tetraurelia parafusin, a phosphoglycoprotein involved in
A Methanococcus vannielii hypothetical protein in the 3'region of the gene
for ribosomal protein S10.
PMM from fungi do not belong to this family.
December 2001 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Dai J.B. Liu Y. Ray W.J. Jr. Konno M.
The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
Koeplin R. Arnold W. Hoette B. Simon R. Wang G. Puehler A.
J. Bacteriol. 174:191-199(1992).
Unpublished observations (1993).
Subramanian S.V. Wyroba E. Andersen A.P. Satir B.H.
Proc. Natl. Acad. Sci. U.S.A. 91:9832-9836(1994).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.