D
IPR005845

Alpha-D-phosphohexomutase, alpha/beta/alpha domain II

InterPro entry
Short nameA-D-PHexomutase_a/b/a-II
Overlapping
homologous
superfamilies
 

Description

This entry represents domain II found in alpha-D-phosphohexomutase enzymes. This domain has a 3-layer α/β/α topology.

The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM), phosphoglucomutase/phosphomannomutase (PGM/PMM), phosphoglucosamine mutase (PNGM), and phosphoacetylglucosamine mutase (PAGM)
[1]
. PGM (
5.4.2.2
) converts D-glucose 1-phosphate into D-glucose 6-phosphate, and participates in both the breakdown and synthesis of glucose
[2]
. PGM/PMM (
5.4.2.2
;
5.4.2.8
) are primarily bacterial enzymes that use either glucose or mannose as substrate, participating in the biosynthesis of a variety of carbohydrates such as lipopolysaccharides and alginate
[3, 4]
. Both PNGM (
5.4.2.3
) and PAGM (
5.4.2.10
) are involved in the biosynthesis of UDP-N-acetylglucosamine
[5, 6]
.

References

1.Functional diversity of the phosphoglucomutase superfamily: structural implications. Levin S, Almo SC, Satir BH. Protein Eng. 12, 737-46, (1999). View articlePMID: 10506283

2.Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution. Liu Y, Ray WJ Jr, Baranidharan S. Acta Crystallogr. D Biol. Crystallogr. 53, 392-405, (1997). View articlePMID: 15299905

3.The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme. Regni C, Schramm AM, Beamer LJ. J. Biol. Chem. 281, 15564-71, (2006). View articlePMID: 16595672

4.Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Regni C, Naught L, Tipton PA, Beamer LJ. Structure 12, 55-63, (2004). View articlePMID: 14725765

5.Identification of the Pseudomonas aeruginosa glmM gene, encoding phosphoglucosamine mutase. Tavares IM, Jolly L, Pompeo F, Leitao JH, Fialho AM, Sa-Correia I, Mengin-Lecreulx D. J. Bacteriol. 182, 4453-7, (2000). View articlePMID: 10913078

6.Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis. Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H. Biochim. Biophys. Acta 1492, 369-76, (2000). View articlePMID: 11004509

Further reading

7. Evolutionary trace analysis of the alpha-D-phosphohexomutase superfamily. Shackelford GS, Regni CA, Beamer LJ. Protein Sci. 13, 2130-8, (2004). View articlePMID: 15238632

GO terms

molecular function

  • None

cellular component

  • None

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.