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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAIn 75
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGydyeIIVVDDGSTDGTAEIARElaarvPRVRVIRLSRNFGKGAAVRAGFKAAR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  76 kgADIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSV--PLKRLLTLKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:cd04179    80 --GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAgmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*
gi 2315514537 154 MSRDAAKKI--EITSDRMEHASQII 176
Cdd:cd04179   158 FRREVLEALlsLLESNGFEFGLELL 182

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAIn 75
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGydyeIIVVDDGSTDGTAEIARElaarvPRVRVIRLSRNFGKGAAVRAGFKAAR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  76 kgADIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSV--PLKRLLTLKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:cd04179    80 --GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAgmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*
gi 2315514537 154 MSRDAAKKI--EITSDRMEHASQII 176
Cdd:cd04179   158 FRREVLEALlsLLESNGFEFGLELL 182

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAinKG 77
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNfeIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRGKAGARNAGLRAA--TG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  78 aDIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSVPLKRLLT----LKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:pfam00535  80 -DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASritlSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ....*...
gi 2315514537 154 MSRDAAKK 161
Cdd:pfam00535 159 YRREALEE 166

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAIn 75
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGydyeIIVVDDGSTDGTAEIARElaarvPRVRVIRLSRNFGKGAAVRAGFKAAR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  76 kgADIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSV--PLKRLLTLKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:cd04179    80 --GDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGSRFVRGGGAgmPLLRRLGSRLFNFLIRLLLGVRISDTQSGFRL 157

                         170       180
                  ....*....|....*....|....*
gi 2315514537 154 MSRDAAKKI--EITSDRMEHASQII 176
Cdd:cd04179   158 FRREVLEALlsLLESNGFEFGLELL 182

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYK---NIVVVDDGSKDNTYEIIKK-SRVHALKHII----NRGQGAALKTGIDYAInk 76
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGidyEIIVVDDNSPDGTAEIVRElAKEYPRVRLIvrpgKRGLGSAYIEGFKAAR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  77 gADIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSV---PLKRLLTLKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:cd06442    79 -GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSRYVEGGGVegwGLKRKLISRGANLLARLLLGRKVSDPTSGFRA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2315514537 154 MSRDAAKKI--EITSDRMEHASQIIEEIYKKRIKYKEVPVT 192
Cdd:cd06442   158 YRREVLEKLidSLVSKGYKFQLELLVRARRLGYRIVEVPIT 198

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAinKG 77
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNfeIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRGKAGARNAGLRAA--TG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  78 aDIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSVPLKRLLT----LKIAILVLWLFYGVKMTDAHNGFRA 153
Cdd:pfam00535  80 -DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASritlSRLPFFLGLRLLGLNLPFLIGGFAL 158

                  ....*...
gi 2315514537 154 MSRDAAKK 161
Cdd:pfam00535 159 YRREALEE 166

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAin 75
Cdd:COG1215    33 VIIPAYNEEAVIEETLRSLLAQDYPKekleVIVVDDGSTDETAEIARElaaeyPRVRVIERPENGGKAAALNAGLKAA-- 110

                          90
                  ....*....|..
gi 2315514537  76 kGADIIVTFDAD 87
Cdd:COG1215   111 -RGDIVVFLDAD 121

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKK-----SRVHALKHIINRGQGAALKTGIDYAinkG 77
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNfeVIVVDDGSTDGTLEILEEyakkdPRVIRVINEENQGLAAARNAGLKAA---R 77

                          90
                  ....*....|
gi 2315514537  78 ADIIVTFDAD 87
Cdd:cd00761    78 GEYILFLDAD 87

dolichyl-phosphate beta-D-mannosyltransferase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537   1 MKIFIVIAAYNESKSISKVINSLKKA--GYKN--IVVVDDGSKDNTYEIIKK-SRVHALKHIINR------GQGAALKTG 69
Cdd:PLN02726    9 MKYSIIVPTYNERLNIALIVYLIFKAlqDVKDfeIIVVDDGSPDGTQDVVKQlQKVYGEDRILLRprpgklGLGTAYIHG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537  70 IDYAinkGADIIVTFDADGQHRVEDIKPMIEPIINKECEITIGSRFLKKTSVP---LKRLLTLKIAILVLWLFYGVKMTD 146
Cdd:PLN02726   89 LKHA---SGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTRYVKGGGVHgwdLRRKLTSRGANVLAQTLLWPGVSD 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315514537 147 AHNGFRAMSRDAAKKIEITSDRMEHASQ--IIEEIYKKRIKYKEVPVTIIYNNYSLSK-GHGGLTQAIKVFTKMFF 219
Cdd:PLN02726  166 LTGSFRLYKRSALEDLVSSVVSKGYVFQmeIIVRASRKGYRIEEVPITFVDRVYGESKlGGSEIVQYLKGLLYLLL 241

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 2315514537   2 KIFIVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEII-----KKSRVHALKHiiNRGQGAALKTGIDY 72
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYPRdrleIIVVSDGSTDGTAEIAreyadKGVKLLRFPE--RRGKAAALNRALAL 107

                          90
                  ....*....|....*
gi 2315514537  73 AinKGaDIIVTFDAD 87
Cdd:cd06439   108 A--TG-EIVVFTDAN 119

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537   5 IVIAAYNESKSISKVINSLKK-AGYKNIVVVDDGSKDNTYEIIKK----SRVHALKHII---NRGQGAALKTGIDY---- 72
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRnKPNFLVLVIDDASDDDTAGIVRLaitdSRVHLLRRHLpnaRTGKGDALNAAYDQirqi 80

                          90       100
                  ....*....|....*....|.
gi 2315514537  73 AINKGAD----IIVTFDADGQ 89
Cdd:cd06436    81 LIEEGADpervIIAVIDADGR 101

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKNI--VVVDDGSKDNTYEIIKKSRVHALKHIINRGQgaalktGIDYAINKG 77
Cdd:cd06433     2 IITPTYNQAETLEETIDSVLSQTYPNIeyIVIDGGSTDGTVDIIKKYEDKITYWISEPDK------GIYDAMNKG 70

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN----IVVVDDGSKDNTYEIIKKSRVHALKHI--INRGQGAALKTGIDYAINKG- 77
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPRelyrIFVVADNCTDDTAQVARAAGATVLERHdpERRGKGYALDFGFRHLLNLAd 80

                          90
                  ....*....|.
gi 2315514537  78 -ADIIVTFDAD 87
Cdd:cd06438    81 dPDAVVVFDAD 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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537   5 IVIAAYNESKSISKVINSLKKAGYK----NIVVVDDGSKDNTYEIIKKSRVHALKHII--------NRGQGAALKTGIDY 72
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPkekfEVILVDDHSTDGTVQILEFAAAKPNFQLKilnnsrvsISGKKNALTTAIKA 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2315514537  73 AINkgaDIIVTFDADGQHRVEDIKPMIEPI 102
Cdd:cd04192    81 AKG---DWIVTTDADCVVPSNWLLTFVAFI 107

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 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKK--SRVHALKHIINRGQGAALKTGIDYAinkGADI 80
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDfeVIVVDNASTDGSVELLRElfPEVRLIRNGENLGFGAGNNQGIREA---KGDY 77

                  ....*..
gi 2315514537  81 IVTFDAD 87
Cdd:cd04186    78 VLLLNPD 84

putative glycosyl transferase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315514537   2 KIFIVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKK-----SRVHALkHIINRGQGAALKTGIDYAI 74
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTAleIIIVNDGSTDNSVEIAKHyaenyPHVRLL-HQANAGVSVARNTGLAVAT 85

                          90
                  ....*....|....
gi 2315514537  75 NKgadiIVTF-DAD 87
Cdd:PRK10073   86 GK----YVAFpDAD 95

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 2315514537   6 VIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEII--KKSRVHALKHIINRGQGAA--LKTGIDYAINKGAD 79
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPdhIIVIDNASTDGTAEWLtsLGDLDNIVYLRLPENLGGAggFYEGVRRAYELGYD 81

                  ....*....
gi 2315514537  80 IIVTFDADG 88
Cdd:cd04185    82 WIWLMDDDA 90

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2315514537   5 IVIAAYNESKSISKVINSLKKAGYKN--IVVVDDGSKDNTYEIIKKSRVHA---LKHI 57
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPfeVIIADDGSTEETKELIEEFKSQFpipIKHV 58

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 2315514537   5 IVIAAYNE-----SKSISKVINSLKKAGYKNIVVVDDGS-------KDNTYEIIKKSRVHALKHIINRGQGAALKTGIDY 72
Cdd:cd02510     2 VIIIFHNEalstlLRTVHSVINRTPPELLKEIILVDDFSdkpelklLLEEYYKKYLPKVKVLRLKKREGLIRARIAGARA 81

                          90
                  ....*....|....
gi 2315514537  73 AInkgADIIVTFDA 86
Cdd:cd02510    82 AT---GDVLVFLDS 92