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 IIA^Gat and IIB^Gat homologues. IIC^Gat is distantly related to IIC^Sgc of E. coli (Reizer et al., 1996); IIA^Gat is distantly related to IIA^Sga and IIA^Sgc of E. coli as well as IIA^Mtl and IIA^Fru. IIB^Gat is distantly related to IIB^Sga and IIB^Sgc of E. coli. Domains in the LicR/CelR family of transcriptional activators show C-terminal domains exhibiting weak sequence similiarity to IIB^Gat and IIA^Gat (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:
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.
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.
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.
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.
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.
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.
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.
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.
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.
Examples:
TC#	Name	Organismal Type	Example
4.A.5.1.1	Galactitol porter	Bacteria	Galactitol IIC-IIB-IIA complex of E. coli

4.A.5.1.2	Pentitol [arabitol (arabinitol, lyxitol)/xylitol] PTS permease, IICBA (encoded within an operon that also encodes a polyol-P dehydrogenase, a ribose-5-P isomerase, a ribulose 5-P-3-epimerase, and a BlgG-type PTS antiterminator) (Saklani-Jusforgues et al., 2001; Kentache et al. 2016).	Bacteria	Arabitol/xylitol IIC-IIB-IIA complex of Listeria monocytogenes IIC (Q71WA6) IIB (Q71WA5) IIA (Q71WA4)

4.A.5.1.3	*Paralogous system of the E. coli* galactitol PTS permease system, SgcABC (SgcC is annotated as a K_pLE2 phage-like element).**	Bacteria	SgcABC of E. coli SgcA (P39363) SgcB (P58035) SgcC (P39365)

4.A.5.1.4	*Paralogous system of the E. coli* galactitol PTS permease system, PTS-galactitol family (Pgf).**	Bacteria	PgfABC of E. coli PgfA (Q8FCM6) PgfB (Q8FCM5) PgfC (Q8FCM4)

4.A.5.1.5	Galactitol enzyme II complex, IIA^Gat- IIB^Gat - IIC^Gat(based on homology)	Archaea	Galactitol-specific enzyme II complex, IIA - IIB - IIC of Haloferax volcanii IIA (D4GUP9) IIB (D4GUQ1) IIC (D4GUQ0)

4.A.5.1.6	Putative galactitol Enzyme II complex of the PTS (IIA^gat, IIB^gat, IIC^gat)	Fusobacteria	Galactitol Enzyme II complex of Leptotrichia hofstadii IIA^gat, 151 aas IIB^gat, 91 aas IIC^gat,444 aas

4.A.5.1.7	Putative pentitol PTS permease, IIABC. Induced by arabitol, but this pentitol did not appear to be a substrate. Encoded within an operon that also encodes a putative polyol-P dehydrogenase and enzymes of the pentose phosphate pathway (PPP) (Kentache et al. 2016).		Putative pentitol group translocator of Listeria monocytogenes IIA, 155 aas IIB, 97 aas IIC, 423 aas