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 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAV---IYVYDNNSTDGTR------AAAKAAGAVVRCEALQGKGHVIRRMFADIEA 78
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAeiarelAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  79 DAYVLVDGDDTYDASAAPAMVAKLLEDQLDMVNGQRVEQAGEGPVGAYRrghRTGNLVLSGLVRAVFGDRIKDMLSGYRV 158
Cdd:cd04179    81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAGMPLLR---RLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*...
gi 2541334821 159 FSRRFVKTFPALAE--GFETETEFTIHA 184
Cdd:cd04179   158 FRREVLEALLSLLEsnGFEFGLELLVGA 185

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 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAV---IYVYDNNSTDGTR------AAAKAAGAVVRCEALQGKGHVIRRMFADIEA 78
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAeiarelAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  79 DAYVLVDGDDTYDASAAPAMVAKLLEDQLDMVNGQRVEQAGEGPVGAYRrghRTGNLVLSGLVRAVFGDRIKDMLSGYRV 158
Cdd:cd04179    81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAGMPLLR---RLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*...
gi 2541334821 159 FSRRFVKTFPALAE--GFETETEFTIHA 184
Cdd:cd04179   158 FRREVLEALLSLLEsnGFEFGLELLVGA 185

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 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAV-IYVYDNNSTDGTR------AAAKAAGAVVRCEALQGKG----HVIRRMFADi 76
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFeIIVVDDGSTDGTVeiaeeyAKKDPRVRVIRLPENRGKAgarnAGLRAATGD- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  77 eadaYVLV-DGDDTYDASAAPAMVAKLLEDQLDMVNGQRVeqAGEGPVGAYRRGHRTGNLVLSGLVRAVFGDRIKDMLSG 155
Cdd:pfam00535  81 ----YIAFlDADDEVPPDWLEKLVEALEEDGADVVVGSRY--VIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154

                         170
                  ....*....|.
gi 2541334821 156 -YRVFSRRFVK 165
Cdd:pfam00535 155 gFALYRREALE 165

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 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAV---IYVYDNNSTDGTR------AAAKAAGAVVRCEALQGKGHVIRRMFADIEA 78
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYdyeIIVVDDGSTDGTAeiarelAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  79 DAYVLVDGDDTYDASAAPAMVAKLLEDQLDMVNGQRVEQAGEGPVGAYRrghRTGNLVLSGLVRAVFGDRIKDMLSGYRV 158
Cdd:cd04179    81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAGMPLLR---RLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*...
gi 2541334821 159 FSRRFVKTFPALAE--GFETETEFTIHA 184
Cdd:cd04179   158 FRREVLEALLSLLEsnGFEFGLELLVGA 185

DPG_synthase is involved in protein N-linked glycosylation; 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAV-----IYVYDNNSTDGTR-------AAAKAAGAVVRCEALQGKGHVIRRMFAD 75
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPsfsyeIIVVDDGSKDGTAevarklaRKNPALIRVLTLPKNRGKGGAVRAGMLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  76 IEADAYVLVDGDDTYDASAAPAMVAKLLEDQLDMVNGQRVEQAGEGPV--GAYRR-GHRTGNLvlsgLVRAVFGDRIKDM 152
Cdd:cd04188    81 ARGDYILFADADLATPFEELEKLEEALKTSGYDIAIGSRAHLASAAVVkrSWLRNlLGRGFNF----LVRLLLGLGIKDT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2541334821 153 LSGYRVFSRRFV-KTFPAL-AEGFETETEFTIHALDLMMPLAELPVCYRERPvGS 205
Cdd:cd04188   157 QCGFKLFTRDAArRLFPRLhLERWAFDVELLVLARRLGYPIEEVPVRWVEIP-GS 210

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 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPG--AVIYVYDNNSTDGTraaakaagaVVRCEALQGKGHVIRRMF---------ADI 76
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGidYEIIVVDDNSPDGT---------AEIVRELAKEYPRVRLIVrpgkrglgsAYI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  77 EA-----DAYVLV-DGDDTYDASAAPAMVAKLLEDQLDMVNGQR-VEQAGEGPVGAYRRG-HRTGNLvlsgLVRAVFGDR 148
Cdd:cd06442    72 EGfkaarGDVIVVmDADLSHPPEYIPELLEAQLEGGADLVIGSRyVEGGGVEGWGLKRKLiSRGANL----LARLLLGRK 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541334821 149 IKDMLSGYRVFSRRFVKTF--PALAEGFETETEFTIHALDLMMPLAELPVCYRERPVGSvSKLrTWSDGLRILRTIVTL 225
Cdd:cd06442   148 VSDPTSGFRAYRREVLEKLidSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGE-SKL-GGKEIVEYLKGLLRL 224

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGA-----VIYVyDNNSTDGTRAAakaagaVVRCEALQGKGHVIR--R-------MF 73
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLgydyeIIFV-DDGSTDRTLEI------LRELAARDPRVKVIRlsRnfgqqaaLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821  74 ADIEA---DAYVLVDGDDTYDASAAPAMVAKLLEDqLDMVNGQRVEqagegpvgayRRGH---RTGNLVLSGLVRAVFGD 147
Cdd:cd04187    74 AGLDHargDAVITMDADLQDPPELIPEMLAKWEEG-YDVVYGVRKN----------RKESwlkRLTSKLFYRLINKLSGV 142

                         170       180
                  ....*....|....*....|....*
gi 2541334821 148 RIKDMLSGYRVFSRRFVKTFPALAE 172
Cdd:cd04187   143 DIPDNGGDFRLMDRKVVDALLLLPE 167

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541334821   8 VLIPCFNEEVAIGKVVADFRTALPGAVIYVYDNNSTDGTraaakaaGAVVRCEALQGKGHVIRR 71
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPNFLVLVIDDASDDDT-------AGIVRLAITDSRVHLLRR 57

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 2541334821   8 VLIPCFNEEVAIGKVVADFRT-ALPGAVIYVYDNNSTDGTR-------AAAKAAGAVVRCEALQGKGHVIRRMFADIEAD 79
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLAlDYPKLEVIVVDDGSTDDTLeileelaALYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                          90       100
                  ....*....|....*....|....*..
gi 2541334821  80 AYVLVDGDDTYDASAAPAMVAKLLEDQ 106
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADP 107

putative glucosyl-3-phosphoglycerate synthase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821   5 RIAVLIPCFNEEVAIGKVVADFRTALPGAV---IYVYDNNSTDGTRAAAKAA-GAVVRCEA-------LQGKGHVIRRMF 73
Cdd:PRK13915   32 TVSVVLPALNEEETVGKVVDSIRPLLMEPLvdeLIVIDSGSTDATAERAAAAgARVVSREEilpelppRPGKGEALWRSL 111

                          90       100       110
                  ....*....|....*....|....*....|
gi 2541334821  74 ADIEADAYVLVDGDDTydaSAAPAMVAKLL 103
Cdd:PRK13915  112 AATTGDIVVFVDADLI---NFDPMFVPGLL 138

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 2541334821   3 PPRIAVLIPCFNEEVAIGKVVAD-FRTALPGAVIYVYDNNSTDGTR-----------AAAKAAGAVVRCEALQGKGHVIR 70
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAiLAQPYPPVEVVVVVNPSDAETLdvaeeiaarfpDVRLRVIRNARLLGPTGKSRGLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2541334821  71 RMFADIEADAYVLVDGDDTYDASAAPAMVAKLLEDQLDMVNGQR 114
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPV 124

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541334821   8 VLIPCFNEEVAIGKVVADFRTAL---PGAVIYVYDNNSTDGTRAAAKAAGAVVrCE----ALQGKGHVIRRMFADI---- 76
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDyprELYRIFVVADNCTDDTAQVARAAGATV-LErhdpERRGKGYALDFGFRHLlnla 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2541334821  77 -EADAYVLVDGDDTYDASAAPAMVAKLledqldmvngqrveQAGEGPVGAYRR 128
Cdd:cd06438    80 dDPDAVVVFDADNLVDPNALEELNARF--------------AAGARVVQAYYN 118