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• 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.

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:

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

Consensus pattern: [GSA]-[LIVMF]-x-[LIVM]-[ST]-[PGA]-S-H-[NIC]-P S is the phosphoserine residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00710 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00710 • Scan Swiss-Prot/TrEMBL entries against PS00710 • view ligand binding statistics

Matching PDB structures: 1C47 1C4G 1KFI 1KFQ ... [ALL]

1	Authors	Dai J.B., Liu Y., Ray W.J. Jr., Konno M.
	Title	The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
	Source	J. Biol. Chem. 267:6322-6337(1992).
	PubMed ID	1532581

2	Authors	Stevenson G., Lee S.J., Romana L.K., Reeves P.R.
	Title	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.
	Source	Mol. Gen. Genet. 227:173-180(1991).
	PubMed ID	1712067

3	Authors	Zielinski N.A., Chakrabarty A.M., Berry A.
	Title	Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase.
	Source	J. Biol. Chem. 266:9754-9763(1991).
	PubMed ID	1903398

4	Authors	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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