Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDNTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90
                 ....*....|...
gi 446448372  93 ypeaDYLLILDAD 105
Cdd:cd02511   73 ----DWVLSLDAD 81

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDNTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90
                 ....*....|...
gi 446448372  93 ypeaDYLLILDAD 105
Cdd:cd02511   73 ----DWVLSLDAD 81

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372   16 CLCMIVKNESRIMERCL----NATKSIVDFVsICDTGSTDNTPEIIENWCKENEIPGTVHHEpfKNFGY--NRSLAVSLA 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLesllNQTYPNFEII-VVDDGSTDGTVEIAEEYAKKDPRVRVIRLP--ENRGKagARNAGLRAA 77

                          90
                  ....*....|....*.
gi 446448372   90 QktypeADYLLILDAD 105
Cdd:pfam00535  78 T-----GDYIAFLDAD 88

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDNTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90
                 ....*....|...
gi 446448372  93 ypeaDYLLILDAD 105
Cdd:cd02511   73 ----DWVLSLDAD 81

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  19 MIVKNESRIMERCLNA----TKSIVDFVsICDTGSTDNTPEIIENWCKENEIPGTVHHEPFKNFGYNRSLAVSLAQktyp 94
Cdd:cd00761    3 IPAYNEEPYLERCLESllaqTYPNFEVI-VVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR---- 77

                         90
                 ....*....|....*
gi 446448372  95 eADYLLILDADMILE 109
Cdd:cd00761   78 -GEYILFLDADDLLL 91

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  21 VKNESRIMERCLNATKSI------VDFVSICDtGSTDNTPEIIENWCKENEIPGTVHHEPFKNFGYNRSLAVSLAQktyp 94
Cdd:COG1215   37 AYNEEAVIEETLRSLLAQdypkekLEVIVVDD-GSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAAR---- 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446448372  95 eADYLLILDADMILE------------------VGPN-------------FDKTSLTEDHYLTL 127
Cdd:COG1215  112 -GDIVVFLDADTVLDpdwlrrlvaafadpgvgaSGANlafrrealeevggFDEDTLGEDLDLSL 174

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  23 NES----RIMERCLNATKSIVDF-VSICDTGSTDNTPEIIENWCKENEIPGTVHHEpfKNFGYNRSL--AVSLAQKtype 95
Cdd:cd04179    7 NEEenipELVERLLAVLEEGYDYeIIVVDDGSTDGTAEIARELAARVPRVRVIRLS--RNFGKGAAVraGFKAARG---- 80

                         90
                 ....*....|.
gi 446448372  96 aDYLLILDADM 106
Cdd:cd04179   81 -DIVVTMDADL 90

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  19 MIVKNESRIMERCL----NATKSIVDF-VSICDTGSTDNTPEIIENWCKENEIPgTVHHEPFKNFGYNRSLAVSLAQkty 93
Cdd:cd02525    6 IPVRNEEKYIEELLesllNQSYPKDLIeIIVVDGGSTDGTREIVQEYAAKDPRI-RLIDNPKRIQSAGLNIGIRNSR--- 81

                         90
                 ....*....|..
gi 446448372  94 peADYLLILDAD 105
Cdd:cd02525   82 --GDIIIRVDAH 91

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372  22 KNESRIMERCLNATKSI----VDFVSICDtGSTDNTPEIIENWCKENEIPGTVHHEP---FK----NFGYNRSlavslaq 90
Cdd:cd06423    6 YNEEAVIERTIESLLALdypkLEVIVVDD-GSTDDTLEILEELAALYIRRVLVVRDKengGKagalNAGLRHA------- 77

                         90
                 ....*....|....*....
gi 446448372  91 ktypEADYLLILDADMILE 109
Cdd:cd06423   78 ----KGDIVVVLDADTILE 92

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448372   22 KNESRIMERCLNATKSI-VDFVSICDTGSTDNTPEIIENWcKENEIPGTVHHEPFKNFGYNRSLAVslaQKTYPEADYLL 100
Cdd:pfam13704   1 RNEADILPQWLAHHLALgFDHIYVYDNGSDDGTAEILARL-PDVSILRSDLSYKDARFQVDWRNAL---LARYAEADWVL 76

                  ....*...
gi 446448372  101 ILDADMIL 108
Cdd:pfam13704  77 VVDADEFL 84