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 446448350  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDHTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446448350  93 ypeaDYLLILDADMILEVD--PEFDKTSLTEDHYLT------------LQYDIHIKYWLTRLLKASLPWKSVGVTHEY 156
Cdd:cd02511   73 ----DWVLSLDADERLTPElaDEILALLATDDYDGYyvprrnfflgrwIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ 146

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 446448350  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDHTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446448350  93 ypeaDYLLILDADMILEVD--PEFDKTSLTEDHYLT------------LQYDIHIKYWLTRLLKASLPWKSVGVTHEY 156
Cdd:cd02511   73 ----DWVLSLDADERLTPElaDEILALLATDDYDGYyvprrnfflgrwIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ 146

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 446448350   16 CLCMIVKNESRIMERCL----NATKSIVDFVsICDTGSTDHTPEIIENWCKENEIPGTVHHEpfKNFGY--NRSLAVSLA 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLesllNQTYPNFEII-VVDDGSTDGTVEIAEEYAKKDPRVRVIRLP--ENRGKagARNAGLRAA 77

                          90       100
                  ....*....|....*....|....*
gi 446448350   90 QktypeADYLLILDADmiLEVDPEF 114
Cdd:pfam00535  78 T-----GDYIAFLDAD--DEVPPDW 95

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 446448350  14 KLCLCMIVKNESRIMERCLNATKSIVDFVSICDTGSTDHTPEIIENwckeneiPG-TVHHEPFKNFGYNRSLAVSLAQKt 92
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKE-------YGaKVYQRWWDGFGAQRNFALELATN- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446448350  93 ypeaDYLLILDADMILEVD--PEFDKTSLTEDHYLT------------LQYDIHIKYWLTRLLKASLPWKSVGVTHEY 156
Cdd:cd02511   73 ----DWVLSLDADERLTPElaDEILALLATDDYDGYyvprrnfflgrwIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ 146

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 446448350   16 CLCMIVKNESRIMERCL----NATKSIVDFVsICDTGSTDHTPEIIENWCKENEIPGTVHHEpfKNFGY--NRSLAVSLA 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLesllNQTYPNFEII-VVDDGSTDGTVEIAEEYAKKDPRVRVIRLP--ENRGKagARNAGLRAA 77

                          90       100
                  ....*....|....*....|....*
gi 446448350   90 QktypeADYLLILDADmiLEVDPEF 114
Cdd:pfam00535  78 T-----GDYIAFLDAD--DEVPPDW 95

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 446448350  23 NES----RIMERCLNATKSIVDF-VSICDTGSTDHTPEIIENWCKENEIPGTVHHEpfKNFGYNRSL--AVSLAQKtype 95
Cdd:cd04179    7 NEEenipELVERLLAVLEEGYDYeIIVVDDGSTDGTAEIARELAARVPRVRVIRLS--RNFGKGAAVraGFKAARG---- 80

                         90
                 ....*....|....*...
gi 446448350  96 aDYLLILDADmiLEVDPE 113
Cdd:cd04179   81 -DIVVTMDAD--LQHPPE 95

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448350  23 NESRIMERCLNATK--SIVDF-VSICDTGSTDHTPEIIENWCKENEIPgtVHHEPFKNFGY----NRSLAVSLAqktypE 95
Cdd:cd06420    7 NRPEALELVLKSVLnqSILPFeVIIADDGSTEETKELIEEFKSQFPIP--IKHVWQEDEGFrkakIRNKAIAAA-----K 79

                         90
                 ....*....|....*.
gi 446448350  96 ADYLLILDADMILEVD 111
Cdd:cd06420   80 GDYLIFIDGDCIPHPD 95

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 446448350  19 MIVKNESRIMERCL----NATKSIVDF-VSICDTGSTDHTPEIIENWCKENEIPgTVHHEPFKNFGYNRSLAVSLAQkty 93
Cdd:cd02525    6 IPVRNEEKYIEELLesllNQSYPKDLIeIIVVDGGSTDGTREIVQEYAAKDPRI-RLIDNPKRIQSAGLNIGIRNSR--- 81

                         90
                 ....*....|..
gi 446448350  94 peADYLLILDAD 105
Cdd:cd02525   82 --GDIIIRVDAH 91

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446448350  44 ICDTGSTDHTPEIIENWCKENEIPGTVHHEPfKNFGYNRSLaVSLAQktYPEADYLLILDAD 105
Cdd:cd04196   32 ISDDGSTDGTVEIIKEYIDKDPFIIILIRNG-KNLGVARNF-ESLLQ--AADGDYVFFCDQD 89