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 1907106004 194 SVILCFHDEAWPTLLRTVHSILDTAPRALLQEIILVDDLSQQELLKSALSEYVAR-LEAVKLLRSNRRLGTIGARMLGAT 272
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 273 RATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVVSPVIDVIDWKTLQYSASK-LHRGTLDWKLDFRWKPLGEQEQKAL 351
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERRRE 160

                  ....*...
gi 1907106004 352 pSPISPVR 359
Cdd:cd02510   161 -SPTAPIR 167

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 194 SVILCFHDEAWPTLLRTVHSILDTAPRALLQEIILVDDLSQQELLKSALSEYVAR-LEAVKLLRSNRRLGTIGARMLGAT 272
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 273 RATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVVSPVIDVIDWKTLQYSASK-LHRGTLDWKLDFRWKPLGEQEQKAL 351
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERRRE 160

                  ....*...
gi 1907106004 352 pSPISPVR 359
Cdd:cd02510   161 -SPTAPIR 167

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 1907106004 180 LCLQQHPTSGLPTASVILCFHDEAwPTLLRTVHSILD-TAPRALLqEIILVDDLSQQELLKsALSEYVARLEAVKLLRSN 258
Cdd:COG1215    18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAqDYPKEKL-EVIVVDDGSTDETAE-IARELAAEYPRVRVIERP 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907106004 259 RRLGTIGARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIADDR 304
Cdd:COG1215    95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 194 SVILCFHDEAWPTLLRTVHSILDTAPRALLQEIILVDDLSQQELLKSALSEYVAR-LEAVKLLRSNRRLGTIGARMLGAT 272
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKyLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 273 RATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVVSPVIDVIDWKTLQYSASK-LHRGTLDWKLDFRWKPLGEQEQKAL 351
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERRRE 160

                  ....*...
gi 1907106004 352 pSPISPVR 359
Cdd:cd02510   161 -SPTAPIR 167

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 1907106004 180 LCLQQHPTSGLPTASVILCFHDEAwPTLLRTVHSILD-TAPRALLqEIILVDDLSQQELLKsALSEYVARLEAVKLLRSN 258
Cdd:COG1215    18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAqDYPKEKL-EVIVVDDGSTDETAE-IARELAAEYPRVRVIERP 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907106004 259 RRLGTIGARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRIADDR 304
Cdd:COG1215    95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140

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 1907106004 195 VILCFHDEAwPTLLRTVHSILD-TAPRallQEIILVDDLSQQELLKsALSEYVARLEAVKLLRSNRRLGTIGARMLGATR 273
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAqTYPN---FEVIVVDDGSTDGTLE-ILEEYAKKDPRVIRVINEENQGLAAARNAGLKA 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907106004 274 ATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVV 308
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADA 110

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 1907106004 195 VILCFHDEAwpTLLRTVHSILDTAPRALLQEIILVDDLSQ---QELLKsalsEYVARLEAVKLLRSNRRLGTIGARMLGA 271
Cdd:cd04179     2 VIPAYNEEE--NIPELVERLLAVLEEGYDYEIIVVDDGSTdgtAEIAR----ELAARVPRVRVIRLSRNFGKGAAVRAGF 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907106004 272 TRATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVV 308
Cdd:cd04179    76 KAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112

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 1907106004 195 VILCFHDEAwPTLLRTVHSILD-TAPRALLqEIILVDDLSQ---QELLKSALSEYVARLeavKLLRSNRRLGTIGARML- 269
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSAlDYPKEKF-EVILVDDHSTdgtVQILEFAAAKPNFQL---KILNNSRVSISGKKNALt 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907106004 270 -GATRATGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVVS-PVI 312
Cdd:cd04192    76 tAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVI 120

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 1907106004 195 VILCFHDEAwPTLLRTVHSILD-TAPRAllqEIILVDDLSQQELLKSALSEYVARLEAVKLLRSNRRLGTIGARMLGATR 273
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLAlDYPKL---EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907106004 274 ATGDVLVFMDAHCECHPGWLEPLLSRIADD 303
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFAD 106

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106004 195 VILCFHDEAwpTLLRTVHSILDTA-PRAllqEIILVDDLSQQELLKSALsEYVARLEAVKL--LRSNRRLGTIGAR--ML 269
Cdd:pfam13641   7 VVPAFNEDS--VLGRVLEAILAQPyPPV---EVVVVVNPSDAETLDVAE-EIAARFPDVRLrvIRNARLLGPTGKSrgLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907106004 270 GATRA-TGDVLVFMDAHCECHPGWLEPLLSRIADDRSRVV 308
Cdd:pfam13641  81 HGFRAvKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAV 120

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 1907106004 225 EIILVDDLSQ---QELLKsalsEYVARLEAVKLLRSNRRLGTIGARMLGATRATGDVLVFMDA---HcecHPGWLEPLLS 298
Cdd:cd06442    29 EIIVVDDNSPdgtAEIVR----ELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDAdlsH---PPEYIPELLE 101

                          90
                  ....*....|
gi 1907106004 299 RIADDRSRVV 308
Cdd:cd06442   102 AQLEGGADLV 111

dolichyl-phosphate beta-glucosyltransferase; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106004 225 EIILVDDLSQQELLKSALS---EYVARLEAVKLLRSNRRLGTIGARMLGATRATGDVLVFMDA 284
Cdd:PTZ00260  109 EIIIVNDGSKDKTLKVAKDfwrQNINPNIDIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDA 171