glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   5 RGGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCM 84
Cdd:cd03796   205 RKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCI 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  85 AIVEAASCGLQVVSTKVGGIPEVLPENLIILCEPSVKSLCEGLEKAIFQVKSGTlPAPENIHNVVKTFYTWRNVAERTEK 164
Cdd:cd03796   285 AIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGK-HDPWSFHNRVKKMYSWEDVARRTEK 363

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807772 165 VYERVSKESVLPMHKRLdRLISHCGPVTGYIFALLA 200
Cdd:cd03796   364 VYDRILSTPNRPFLERL-KRYYNCGPIAGKIFCLLA 398

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   5 RGGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCM 84
Cdd:cd03796   205 RKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCI 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  85 AIVEAASCGLQVVSTKVGGIPEVLPENLIILCEPSVKSLCEGLEKAIFQVKSGTlPAPENIHNVVKTFYTWRNVAERTEK 164
Cdd:cd03796   285 AIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGK-HDPWSFHNRVKKMYSWEDVARRTEK 363

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807772 165 VYERVSKESVLPMHKRLdRLISHCGPVTGYIFALLA 200
Cdd:cd03796   364 VYDRILSTPNRPFLERL-KRYYNCGPIAGKIFCLLA 398

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  71 HIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI-ILCEP-SVKSLCEGLEKAIfqvKSGTLPA--PENIH 146
Cdd:COG0438    22 DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPgDPEALAEAILRLL---EDPELRRrlGEAAR 98

                          90       100
                  ....*....|....*....|....*
gi 1958807772 147 NVVKTFYTWRNVAERTEKVYERVSK 171
Cdd:COG0438    99 ERAEERFSWEAIAERLLALYEELLA 123

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958807772   72 IFLNTSLTEAFCMAIVEAASCGLQVVSTKVGG---IPEVLPENLII 114
Cdd:TIGR02468  574 VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGpvdIHRVLDNGLLV 619

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   5 RGGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCM 84
Cdd:cd03796   205 RKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCI 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  85 AIVEAASCGLQVVSTKVGGIPEVLPENLIILCEPSVKSLCEGLEKAIFQVKSGTlPAPENIHNVVKTFYTWRNVAERTEK 164
Cdd:cd03796   285 AIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPEDIVRKLEEAISILRTGK-HDPWSFHNRVKKMYSWEDVARRTEK 363

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807772 165 VYERVSKESVLPMHKRLdRLISHCGPVTGYIFALLA 200
Cdd:cd03796   364 VYDRILSTPNRPFLERL-KRYYNCGPIAGKIFCLLA 398

Glycosyl transferases group 1;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   7 GTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVREryqLHDRVQLLGALEhkDVRNVLVQGHIFLNTSLTEAFCMAI 86
Cdd:pfam13692  16 GVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAG---LEDRVIFTGFVE--DLAELLAAADVFVLPSLYEGFGLKL 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807772  87 VEAASCGLQVVSTKVGGIPEVLPENLIILCEP-SVKSLCEGLEKAI 131
Cdd:pfam13692  91 LEAMAAGLPVVATDVGGIPELVDGENGLLVPPgDPEALAEAILRLL 136

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   3 NRRGGTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAF 82
Cdd:cd03798   210 IPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGF 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  83 CMAIVEAASCGLQVVSTKVGGIPEVL-PENLIILCEP-SVKSLCEGLEKAIFQVKSGTLPApENIHNVVKTFyTWRNVAE 160
Cdd:cd03798   290 GLVLLEAMACGLPVVATDVGGIPEVVgDPETGLLVPPgDADALAAALRRALAEPYLRELGE-AARARVAERF-SWVKAAD 367

                  ....*....
gi 1958807772 161 RTEKVYERV 169
Cdd:cd03798   368 RIAAAYRDV 376

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   7 GTDLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQG-HIFLNTSLTEAFCMA 85
Cdd:cd01635   124 GIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLPSRSEGFGLV 203

                          90       100
                  ....*....|....*....|....*.
gi 1958807772  86 IVEAASCGLQVVSTKVGGIPEVLPEN 111
Cdd:cd01635   204 LLEAMAAGKPVIATDVGGIPEFVVDG 229

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  21 KYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTK 100
Cdd:cd03811   216 KYPDVKLVILGDGPLREELEKLAKELGLAERVIFLG--FQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD 293

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958807772 101 VGGIPEVLPENL-IILCEPSVKSLCEGLEKAIFQVK 135
Cdd:cd03811   294 CPGPREILDDGEnGLLVPDGDAAALAGILAALLQKK 329

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  31 GEGPKRIILEEVRERYQLHDRVQLLGALEHkdVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPE 110
Cdd:cd04962   233 GDGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKH 310

                  .
gi 1958807772 111 N 111
Cdd:cd04962   311 G 311

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  15 IPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGAleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGL 94
Cdd:cd04951   210 ISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQ--ISNISEYYNAADLFVLSSEWEGFGLVVAEAMACER 287

                          90       100
                  ....*....|....*....|.
gi 1958807772  95 QVVSTKVGGIPEVL-PENLII 114
Cdd:cd04951   288 PVVATDAGGVAEVVgDHNYVV 308

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  27 FLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPE 106
Cdd:cd03817   234 LVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASE 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807772 107 VLpENLI--ILCEPSVKSLCEGLEKAIFQVKSGTLPApENIHNVVKTFytwrNVAERTEKVYERV 169
Cdd:cd03817   314 LV-EDGEngFLFEPNDETLAEKLLHLRENLELLRKLS-KNAEISAREF----AFAKSVEKLYEEV 372

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  18 LCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLT------EAFCMAIVEAAS 91
Cdd:cd03799   199 LAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTaadgdqDGPPNTLKEAMA 278

                          90       100
                  ....*....|....*....|.
gi 1958807772  92 CGLQVVSTKVGGIPEVLPENL 112
Cdd:cd03799   279 MGLPVISTEHGGIPELVEDGV 299

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  28 LIGGEGPKRIILEEVRERYqlhDRVQLLGALEHKDVRNVLVQGHIFLNTSLT------EAFCMAIVEAASCGLQVVSTKV 101
Cdd:cd05844   224 VIAGDGPLRPALQALAAAL---GRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRH 300

                  ....*
gi 1958807772 102 GGIPE 106
Cdd:cd05844   301 GGIPE 305

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  23 QELNF--LIGGEGPKRIILEEVRErYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSL--TEAFCMAIVEAASCGLQVVS 98
Cdd:cd03795   214 QYLNYpiVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVIS 292

                  ....*
gi 1958807772  99 TKVGG 103
Cdd:cd03795   293 TNIGT 297

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  27 FLIGGEGPKRiilEEVRERYqlhDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPE 106
Cdd:cd03814   231 LVVVGDGPAR---AELEARG---PDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRD 304

                  ....
gi 1958807772 107 VLPE 110
Cdd:cd03814   305 IVRP 308

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772   9 DLLSGIIPELCQKYQELNFLIGGEGPKRIILEEVRERYQLHDRVQLLGAleHKDVRNVLVQGHIFLNTSLTEAFCMAIVE 88
Cdd:cd04949   176 DHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQMEGFGLTLME 253

                          90
                  ....*....|...
gi 1958807772  89 AASCGLQVVSTKV 101
Cdd:cd04949   254 AIGHGLPVVSYDV 266

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  28 LIGGEGPKRIILEEVRERYQ---LHDRVQLLGaleHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGI 104
Cdd:cd03813   329 LIGPEDEDPEYAQECKRLVAslgLENKVKFLG---FQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSC 405

                  ....
gi 1958807772 105 PEVL 108
Cdd:cd03813   406 RELI 409

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807772  50 DRVQLLGALEHKDVRNVLVQGHIFLNTSL-TEAFCMAIVEAASCGLQVVSTKVGGIPEVLPENLI-ILCEPSvkslcEGL 127
Cdd:cd03802   220 PRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETgFLVDSV-----EEM 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958807772 128 EKAIFQVksGTLPaPENIHNVVKTFYTWRNVAERTEKVYERV 169
Cdd:cd03802   295 AEAIANI--DRID-RAACRRYAEDRFSAARMADRYEALYRKV 333

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807772  31 GEGPKRI-ILEEVRERyQLHDRVQLLGalEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVV 97
Cdd:cd03812   229 GEGELKEkIKEKVKEL-GLEDKVIFLG--FRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293