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4.A.5 The PTS Galactitol (Gat) Family

The only well-characterized member of the Gat famly is the galactitol permease of E. coli (Noblemann and Lengeler, 1995). However, a homologous IIC protein (38% identity) from Listeria monocytogenes has been shown to be required for D-arabitol fermentation (Saklani-Jusforgues et al., 2001). It functions together with IIAGat and IIBGat homologues. IICGat is distantly related to IICSgc of E. coli (Reizer et al., 1996); IIAGat is distantly related to IIASga and IIASgc of E. coli as well as IIAMtl and IIAFru. IIBGat is distantly related to IIBSga and IIBSgc of E. coli. Domains in the LicR/CelR family of transcriptional activators show C-terminal domains exhibiting weak sequence similiarity to IIBGat and IIAGat (Tchieu et al., 2001). The biochemistry of this family is poorly defined. Howeever, the 3-d structure of GatB has been solved. GatB consists of a central four-stranded parallel beta-sheet flanked by alpha-helices on both sides. The active site cysteine of GatB is located at the beginning of an unstructured loop between beta1 and alpha1 that folds into a P-loop-like structure. This structural arrangement shows similarities with other IIB subunits as noted above, but also with mammalian low molecular weight protein tyrosine phosphatases (LMW PTPase) and arsenate reductase (ArsC) (Volpon et al. 2006).The Gat Family is related to the L-Asc Family (TC# 4.A.7) (Hvorup et al. 2003; Saier et al. 2005).

This family belongs to the: PTS-AG Superfamily.

References associated with 4.A.5 family:

Hvorup, R., A.B. Chang, and M.H. Saier, Jr. (2003). Bioinformatic analyses of the bacterial L-ascorbate phosphotransferase system permease family. J. Mol. Microbiol. Biotechnol. 6: 191-205. 15153772
Kentache, T., E. Milohanic, T.N. Cao, A. Mokhtari, F.M. Aké, Q.M. Ma Pham, P. Joyet, and J. Deutscher. (2016). Transport and Catabolism of Pentitols by Listeria monocytogenes. J. Mol. Microbiol. Biotechnol. 26: 369-380. 27553222
Noblemann, B. and J.W. Lengeler. (1995). Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262: 69-72. 7772602
Noblemann, B. and J.W. Lengeler. (1996). Molecular analysis of the gat genes from Escherichia coli and their roles in galactitol transport and metabolism. J. Bacteriol. 178: 6790-6795.
Reizer, J., A. Reizer, and M.H. Saier, Jr. (1997). Is the ribulose monophosphate pathway widely distributed in bacteria? Microbiology 143: 2519-2520. 9274005
Reizer, J., A. Reizer, M.J. Merrick, G. Plunkett, 3rd, D.J. Rose, and M.H. Saier, Jr. (1996). Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain. Gene 181: 103-108. 8973315
Saier, M.H., R.N. Hvorup, and R.D. Barabote. (2005). Evolution of the bacterial phosphotransferase system: from carriers and enzymes to group translocators. Biochem Soc Trans 33: 220-224. 15667312
Saklani-Jusforgues, H., E. Fontan, and P.L. Goossens. (2001). Characterisation of a Listeria monocytogenes mutant deficient in D-arabitol fermentation. Res. Microbiol. 152: 175-177. 11316371
Tchieu, J.H., V. Norris, J.S. Edwards, and M.H. Saier, Jr. (2001). The complete phosphotransferase system in Escherichia coli. J. Mol. Microbiol. Biotechnol. 3: 329-346. 11361063
Volpon, L., C.R. Young, A. Matte, and K. Gehring. (2006). NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA. Protein. Sci. 15: 2435-2441. 16963640