To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00589

Phosphoglucomutase and phosphomannomutase phosphoserine signature





Description
  • 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.
Note:

PMM from fungi do not belong to this family.

Last update:

December 2001 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PGM_PMM, PS00710; Phosphoglucomutase and phosphomannomutase phosphoserine signature  (PATTERN)


References

1AuthorsDai J.B., Liu Y., Ray W.J. Jr., Konno M.
TitleThe crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
SourceJ. Biol. Chem. 267:6322-6337(1992).
PubMed ID1532581

2AuthorsStevenson G., Lee S.J., Romana L.K., Reeves P.R.
TitleThe 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.
SourceMol. Gen. Genet. 227:173-180(1991).
PubMed ID1712067

3AuthorsZielinski N.A., Chakrabarty A.M., Berry A.
TitleCharacterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase.
SourceJ. Biol. Chem. 266:9754-9763(1991).
PubMed ID1903398

4AuthorsKoeplin R., Arnold W., Hoette B., Simon R., Wang G., Puehler A.
SourceJ. Bacteriol. 174:191-199(1992).

5AuthorsBairoch A.
SourceUnpublished observations (1993).

6AuthorsSubramanian S.V., Wyroba E., Andersen A.P., Satir B.H.
SourceProc. 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
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)