Phosphoglucomutase (EC 5.4.2.2) (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 [1].
Phosphomannomutase (EC 5.4.2.8) (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 [2]. In Pseudomonas aeruginosa PMM
(gene algC) is involved in the biosynthesis of the alginate layer [3] and
in Xanthomonas campestris (gene xanA) it is involved in the biosynthesis of
xanthan [4]. In Rhizobium strain ngr234 (gene noeK) it is involved in the
biosynthesis of the nod factor.
Phosphoacetylglucosamine mutase (EC 5.4.2.3) 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 [1]. 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
exocytosis.
A Methanococcus vannielii hypothetical protein in the 3'region of the gene
for ribosomal protein S10.
The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster.
Koeplin R. Arnold W. Hoette B. Simon R. Wang G. Puehler A.
Source
J. Bacteriol. 174:191-199(1992).
5
Authors
Bairoch A.
Source
Unpublished observations (1993).
6
Authors
Subramanian S.V. Wyroba E. Andersen A.P. Satir B.H.
Source
Proc. Natl. Acad. Sci. U.S.A. 91:9832-9836(1994).
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