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 1233016389   5 VFTPAFNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNFeIQYIYKKNGGMHTAHNTAYENIYTE 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRV-IRVINEENQGLAAARNAGLKAARGE 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1233016389  85 LNVCIDSDDYMPEDAVELILEKWSKIKNKGYAGIVG 120
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPG 115

putative glycosyl transferase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233016389   2 LLTVFTPAFNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNFEIqyIYKKNGGMHTAHNT 76
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRL--LHQANAGVSVARNT 79

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 1233016389   5 VFTPAFNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNFeIQYIYKKNGGMHTAHNTAYENIYTE 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRV-IRVINEENQGLAAARNAGLKAARGE 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1233016389  85 LNVCIDSDDYMPEDAVELILEKWSKIKNKGYAGIVG 120
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPG 115

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 1233016389   5 VFTPAFNRAHTLIRTYKSLQAQTCKDFIW--LVVDDGSTDNTAELICSWKKENNNFEIqYIYKKNGGMHTAHNTAYENIY 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYeiIVVDDGSTDGTAEIARELAARVPRVRV-IRLSRNFGKGAAVRAGFKAAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1233016389  83 TELNVCIDSDD-YMPEDAVELIlekwSKIKNKGYAGIVG 120
Cdd:cd04179    80 GDIVVTMDADLqHPPEDIPKLL----EKLLEGGADVVIG 114

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 1233016389   1 MLLTVFTPAFNRAHTLIRTYKSLQAQTCKDFIW--LVVDDGSTDNTAELICSWKKENNNFEIQYIyKKNGGMHTAHNTAY 78
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLevIVVDDGSTDETAEIARELAAEYPRVRVIER-PENGGKAAALNAGL 107

                          90       100
                  ....*....|....*....|....*..
gi 1233016389  79 ENIYTELNVCIDSDDYMPEDAVELILE 105
Cdd:COG1215   108 KAARGDIVVFLDADTVLDPDWLRRLVA 134

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389  10 FNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELIcswKKENNNFEIQYIY-KKN----GGMHTAHNTAYENIYTE 84
Cdd:cd04185     6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWL---TSLGDLDNIVYLRlPENlggaGGFYEGVRRAYELGYDW 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1233016389  85 lnVCIDSDDYMPE-DAVELILEKWSKIKNKGYAGIVgLDADSC 126
Cdd:cd04185    83 --IWLMDDDAIPDpDALEKLLAYADKDNPQFLAPLV-LDPDGS 122

putative glycosyl transferase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233016389   2 LLTVFTPAFNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNFEIqyIYKKNGGMHTAHNT 76
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRL--LHQANAGVSVARNT 79

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   8 PAFNRAHTLIRTYKSLQAQTCKD--FIWLVVDDGSTDNTAELIcSWKKENNNFEIQYI---YKKNGGMHTAHNTAYENIY 82
Cdd:cd04192     4 AARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQIL-EFAAAKPNFQLKILnnsRVSISGKKNALTTAIKAAK 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1233016389  83 TELNVCIDSDDYMPEDAVELILEKWSKIKNKGYAGIV 119
Cdd:cd04192    83 GDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPV 119

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233016389   5 VFTPAFNRAHTLIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKEnNNFEIQYIYKKNGG 69
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQ-FPIPIKHVWQEDEG 64

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   2 LLTVFTPAFNRAHT-LIRTYKSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNfEIQYIY-KKNGGMHTAHNTAYE 79
Cdd:cd04184     2 LISIVMPVYNTPEKyLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDP-RIKVVFrEENGGISAATNSALE 80

                          90       100
                  ....*....|....*....|
gi 1233016389  80 NIYTELNVCIDSDDYMPEDA 99
Cdd:cd04184    81 LATGEFVALLDHDDELAPHA 100

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   4 TVFTPAFNRAHTLIRTYKSLQAQtckDFIW-----LVVDDGSTDNTAELICSWKKENNNFeiqYIYKKNGGMHTAHNTAY 78
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLLAL---DYPRdrleiIVVSDGSTDGTAEIAREYADKGVKL---LRFPERRGKAAALNRAL 105

                          90       100
                  ....*....|....*....|....*.
gi 1233016389  79 ENIYTELNVCIDSDDYMPEDAVELIL 104
Cdd:cd06439   106 ALATGEIVVFTDANALLDPDALRLLV 131

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1233016389   3 LTVFTPAFNRAHTLIRTYKSLQAQT-CKDFIW--LVVDDGSTDNTAELI 48
Cdd:NF038302    3 FTVAIPTYNGANRLPEVLERLRSQIgTESLSWeiIVVDNNSTDNTAQVV 51

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389  21 KSLQAQTCKDFIWLVVDDGSTDNTAELICSWKKENNNFEIQYIYKKNGGmhtahntAYENIYTELNVC-------IDSDD 93
Cdd:cd04196    18 DSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLG-------VARNFESLLQAAdgdyvffCDQDD 90

                          90
                  ....*....|....*.
gi 1233016389  94 YMPEDAVELILEKWSK 109
Cdd:cd04196    91 IWLPDKLERLLKAFLK 106

dolichyl-phosphate beta-glucosyltransferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   3 LTVFTPAFNRAHTLIRTYKS----LQAQTCKD--FIW--LVVDDGSTDNTAELICSW--KKENNNFEIQYI-YKKNGGMH 71
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKEtikyLESRSRKDpkFKYeiIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLsLLRNKGKG 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1233016389  72 TAHNTAYENIYTELNVCIDSDDYMPEDAVELILEKWSKIKNKGYAGIVG 120
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQNGLGIVFG 200

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   5 VFTPAFNRAHTLIRTYKSLQAqTCKDFIW--LVVDDGSTDNTAELICSWKKENNNFEIQyIYKKNGGMHTAHNTAYENIY 82
Cdd:cd06442     1 IIIPTYNERENIPELIERLDA-ALKGIDYeiIVVDDNSPDGTAEIVRELAKEYPRVRLI-VRPGKRGLGSAYIEGFKAAR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1233016389  83 TELNVCIDSD---DymPEDAVELIlekwSKIKNKGYAGIVG 120
Cdd:cd06442    79 GDVIVVMDADlshP--PEYIPELL----EAQLEGGADLVIG 113

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233016389   5 VFTPAFNRAHTLIRTYKSLQAQTCKDFIWL-VVDDGSTDNTAELICSWKK--ENNNFEIQYIYKKNG---GMHTAHNTAY 78
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELsVFNDASTDKSAEIIEKWRKklEDSGVIVLVGSHNSPspkGVGYAKNQAI 80

                          90       100
                  ....*....|....*....|....*..
gi 1233016389  79 ENIYTELNVCIDSDDYMPEDAVELILE 105
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYE 107