NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2205656896|ref|WP_240781825|]
View 

MULTISPECIES: glycosyltransferase family 4 protein [Saccharolobus]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-368 1.65e-28

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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 certain bacteria and archaea.


:

Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 114.17  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896   4 LLYINVGNPAVSGATMIVTELLSRLPTKGVKVDLIellfkedegLLGRYPELNEKVNVIDIIRIPYSGNLAGRFIRyiyk 83
Cdd:cd03801     3 LLLSPELPPPVGGAERHVRELARALAARGHDVTVL---------TPADPGEPPEELEDGVIVPLLPSLAALLRARR---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  84 nIILKRKIGNLIDNYDFII--GINTAKSIRMLYLEPFITFPLYKHYLNLIRITNIIDGTAWFIDsvKGFRESKRNKLNIC 161
Cdd:cd03801    70 -LLRELRPLLRLRKFDVVHahGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLA--RAEALLRRADAVIA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 162 LGSVLSKMVKTKYGIECEALDP-PGGVDPN-----LVKDVTPFPENFDAIHLARQGFMKGTPEVIQIMKNLKKYGYK-KF 234
Cdd:cd03801   147 VSEALRDELRALGGIPPEKIVViPNGVDLErfsppLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 235 AIIG--GQDYGFDINKYLDDKDIVYFGEILDKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYY 312
Cdd:cd03801   227 VIVGgdGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656896 313 GDCEAVKLVKEGDVEGmMSEAL-KIINNNEYYKSLA----FKCISKYTWDKVAESFVQILH 368
Cdd:cd03801   307 EDGEGGLVVPPDDVEA-LADALlRLLADPELRARLGraarERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-368 1.65e-28

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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 certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 114.17  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896   4 LLYINVGNPAVSGATMIVTELLSRLPTKGVKVDLIellfkedegLLGRYPELNEKVNVIDIIRIPYSGNLAGRFIRyiyk 83
Cdd:cd03801     3 LLLSPELPPPVGGAERHVRELARALAARGHDVTVL---------TPADPGEPPEELEDGVIVPLLPSLAALLRARR---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  84 nIILKRKIGNLIDNYDFII--GINTAKSIRMLYLEPFITFPLYKHYLNLIRITNIIDGTAWFIDsvKGFRESKRNKLNIC 161
Cdd:cd03801    70 -LLRELRPLLRLRKFDVVHahGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLA--RAEALLRRADAVIA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 162 LGSVLSKMVKTKYGIECEALDP-PGGVDPN-----LVKDVTPFPENFDAIHLARQGFMKGTPEVIQIMKNLKKYGYK-KF 234
Cdd:cd03801   147 VSEALRDELRALGGIPPEKIVViPNGVDLErfsppLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 235 AIIG--GQDYGFDINKYLDDKDIVYFGEILDKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYY 312
Cdd:cd03801   227 VIVGgdGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656896 313 GDCEAVKLVKEGDVEGmMSEAL-KIINNNEYYKSLA----FKCISKYTWDKVAESFVQILH 368
Cdd:cd03801   307 EDGEGGLVVPPDDVEA-LADALlRLLADPELRARLGraarERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 270-369 8.25e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 84.27  E-value: 8.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 270 ILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFK 349
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....
gi 2205656896 350 CI----SKYTWDKVAESFVQILHK 369
Cdd:COG0438    97 AReraeERFSWEAIAERLLALYEE 120
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 204-347 4.21e-16

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 75.00  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 204 AIHLARQGFMKGTPEVIQIMKNLKKYGYK-KFAIIGGQDYgFDINKYLDDK-----DIVYFGEIlDKKRIYSILKSSKIF 277
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNlKLVIAGDGEE-EKRLKKLAEKlglgdNVIFLGFV-SDEDLPELLKIADVF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656896 278 IYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEgMMSEAL-KIINNNEYYKSLA 347
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAE-ALAEAIdKLLEDEELRERLG 152
thiol_BshA TIGR03999
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ...
 253-343 3.34e-10

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274914 [Multi-domain]  Cd Length: 374  Bit Score: 61.08  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 253 KDIVYFGEILDKKRIYSIlksSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRyyygdcEAVK------LVKEGDV 326
Cdd:TIGR03999 255 DRVLFLGKQDDVAELLSI---SDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIP------EVVEhgvtgfLCDVGDV 325

                          90
                  ....*....|....*..
gi 2205656896 327 EGMMSEALKIINNNEYY 343
Cdd:TIGR03999 326 ETMAEYAISLLEDEELL 342
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 199-356 3.01e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.86  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 199 PENFDAIHLARQGFMKGTPEVIQIMKNLKKygyKKFAIIGGQDYGFDINKYLDDKDIVYFGeILDKKRIYSILKSSKIFI 278
Cdd:PLN02871  261 PEKPLIVYVGRLGAEKNLDFLKRVMERLPG---ARLAFVGDGPYREELEKMFAGTPTVFTG-MLQGDELSQAYASGDVFV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 279 YPTHVDSFGIVIAEALACGVPVIAY---DLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFKC---IS 352
Cdd:PLN02871  337 MPSESETLGFVVLEAMASGVPVVAAragGIPDIIPPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAreeVE 416


                  ....
gi 2205656896 353 KYTW 356
Cdd:PLN02871  417 KWDW 420
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-368 1.65e-28

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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 certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 114.17  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896   4 LLYINVGNPAVSGATMIVTELLSRLPTKGVKVDLIellfkedegLLGRYPELNEKVNVIDIIRIPYSGNLAGRFIRyiyk 83
Cdd:cd03801     3 LLLSPELPPPVGGAERHVRELARALAARGHDVTVL---------TPADPGEPPEELEDGVIVPLLPSLAALLRARR---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  84 nIILKRKIGNLIDNYDFII--GINTAKSIRMLYLEPFITFPLYKHYLNLIRITNIIDGTAWFIDsvKGFRESKRNKLNIC 161
Cdd:cd03801    70 -LLRELRPLLRLRKFDVVHahGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLA--RAEALLRRADAVIA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 162 LGSVLSKMVKTKYGIECEALDP-PGGVDPN-----LVKDVTPFPENFDAIHLARQGFMKGTPEVIQIMKNLKKYGYK-KF 234
Cdd:cd03801   147 VSEALRDELRALGGIPPEKIVViPNGVDLErfsppLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvRL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 235 AIIG--GQDYGFDINKYLDDKDIVYFGEILDKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYY 312
Cdd:cd03801   227 VIVGgdGPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656896 313 GDCEAVKLVKEGDVEGmMSEAL-KIINNNEYYKSLA----FKCISKYTWDKVAESFVQILH 368
Cdd:cd03801   307 EDGEGGLVVPPDDVEA-LADALlRLLADPELRARLGraarERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 270-369 8.25e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 84.27  E-value: 8.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 270 ILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFK 349
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....
gi 2205656896 350 CI----SKYTWDKVAESFVQILHK 369
Cdd:COG0438    97 AReraeERFSWEAIAERLLALYEE 120
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 204-347 4.21e-16

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 75.00  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 204 AIHLARQGFMKGTPEVIQIMKNLKKYGYK-KFAIIGGQDYgFDINKYLDDK-----DIVYFGEIlDKKRIYSILKSSKIF 277
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNlKLVIAGDGEE-EKRLKKLAEKlglgdNVIFLGFV-SDEDLPELLKIADVF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656896 278 IYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEgMMSEAL-KIINNNEYYKSLA 347
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAE-ALAEAIdKLLEDEELRERLG 152
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 214-362 9.33e-16

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 77.79  E-value: 9.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 214 KGTPEVIQIMKNLKKYGYK-KFAIIGGQDYGFD-----INKYLDDKDIVYFGEILDKKrIYSILKSSKIFIYPTHVDSFG 287
Cdd:cd03809   205 KNHERLLKAFALLKKQGGDlKLVIVGGKGWEDEelldlVKKLGLGGRVRFLGYVSDED-LPALYRGARAFVFPSLYEGFG 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656896 288 IVIAEALACGVPVIAYDLPAIRYYYGDceAVKLVKEGDVEGMMSEALKIINNNEYYKSLA---FKCISKYTWDKVAES 362
Cdd:cd03809   284 LPVLEAMACGTPVIASNISVLPEVAGD--AALYFDPLDPESIADAILRLLEDPSLREELIrkgLERAKKFSWEKTAEK 359
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 254-369 5.54e-14

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 72.36  E-value: 5.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 254 DIVYFGEILDKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGmMSEA 333
Cdd:cd03825   244 DIISLGYIDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQA-LAEA 322

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2205656896 334 LK-IINNNEYYKSLAFKCISK----YTWDKVAESFVQILHK 369
Cdd:cd03825   323 IEwLLANPKERESLGERARALaenhFDQRVQAQRYLELYKD 363
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
214-339 6.30e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 65.23  E-value: 6.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 214 KGTPEVIQIMKNLKKYGYK-KFAIIGGQDYGFDINKYLDDKDIVYF-GEILDKKRIYsilKSSKIFIYPTHVDSFGIVIA 291
Cdd:pfam13692  15 KGVDYLLEAVPLLRKRDNDvRLVIVGDGPEEELEELAAGLEDRVIFtGFVEDLAELL---AAADVFVLPSLYEGFGLKLL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2205656896 292 EALACGVPVIAYDLPAIRyyygdcEAVK-----LVKEGDVEGMMSEALKIINN 339
Cdd:pfam13692  92 EAMAAGLPVVATDVGGIP------ELVDgenglLVPPGDPEALAEAILRLLED 138
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 16-347 1.70e-12

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.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 67.77  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  16 GATMIVTELLSRLPTKGVKVDLielLFKEDEGLLGRYPELNEKVNVIDIIRIPYSGNLAGRFIRYIYKNIIlkrkignlI 95
Cdd:cd03811    13 GAERVLLNLANALDKRGYDVTL---VLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILK--------R 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  96 DNYDFIIGINTAKSIrmlylepFITFPLYKHYLNLIRITNIIDGtawfIDSVKGFRESKRNKLNIC--LGSVlSKMVKTK 173
Cdd:cd03811    82 AKPDVVISFLGFATY-------IVAKLAAARSKVIAWIHSSLSK----LYYLKKKLLLKLKLYKKAdkIVCV-SKGIKED 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 174 YgIECEALDP------PGGVDPNLVK---DVTPFPENFDA---IHLARQGFMKGTPEVIQIMKNLKKYGYK-KFAIIG-G 239
Cdd:cd03811   150 L-IRLGPSPPekieviYNPIDIDRIRalaKEPILNEPEDGpviLAVGRLDPQKGHDLLIEAFAKLRKKYPDvKLVILGdG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 240 QDYGfDINKY---LDDKDIVYF-GEildKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDC 315
Cdd:cd03811   229 PLRE-ELEKLakeLGLAERVIFlGF---QSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDG 304

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2205656896 316 EAVKLVKEGDVEGMMSEALKIINNNEYYKSLA 347
Cdd:cd03811   305 ENGLLVPDGDAAALAGILAALLQKKLDAALRE 336
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 214-346 4.93e-12

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 66.46  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 214 KGTPEVIQIMKNLKKYGYK-KFAIIGGQD----YGFDINKYLDDKDIVYFGEILDKKRIYSilkSSKIFIYPTHVDSFGI 288
Cdd:cd03808   202 KGIDELIEAAKILKKKGPNvRFLLVGDGElenpSEILIEKLGLEGRIEFLGFRSDVPELLA---ESDVFVLPSYREGLPR 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205656896 289 VIAEALACGVPVIAYDLPAIRyyygdcEAVK------LVKEGDVEGMMSEALKIINNNEYYKSL 346
Cdd:cd03808   279 SLLEAMAAGRPVITTDVPGCR------ELVIdgvngfLVPPGDVEALADAIEKLIEDPELRKEM 336
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 202-321 5.89e-12

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 64.73  E-value: 5.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 202 FDAIHLARQGFMKGTPEVIQIMKNLKKYGYK-KFAIIGGQDYGFDINKYL----DDKDIVYFGEILDKKRIYSILKSSKI 276
Cdd:cd01635   111 ADKVSVGRLVPEKGIDLLLEALALLKARLPDlVLVLVGGGGEREEEEALAaalgLLERVVIIGGLVDDEVLELLLAAADV 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2205656896 277 FIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLV 321
Cdd:cd01635   191 FVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 214-365 7.51e-11

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 63.16  E-value: 7.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 214 KGTPEVIQIMKNLKKYGYKKFAIIGGQDYG------FDINKYLDDKDIVYFGEILDKKRIySILKSSKIFIYPTHVDSFG 287
Cdd:cd03821   217 KGLDLLIRAARKLAEQGRDWHLVIAGPDDGaypaflQLQSSLGLGDRVTFTGPLYGEAKW-ALYASADLFVLPSYSENFG 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 288 IVIAEALACGVPVIAYDLPAI-RYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFKCI---SKYTWDKVAESF 363
Cdd:cd03821   296 NVVAEALACGLPVVITDKCGLsELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARqveENFSWEAVAGQL 375


                  ..
gi 2205656896 364 VQ 365
Cdd:cd03821   376 GE 377
thiol_BshA TIGR03999
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ...
 253-343 3.34e-10

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274914 [Multi-domain]  Cd Length: 374  Bit Score: 61.08  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 253 KDIVYFGEILDKKRIYSIlksSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRyyygdcEAVK------LVKEGDV 326
Cdd:TIGR03999 255 DRVLFLGKQDDVAELLSI---SDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIP------EVVEhgvtgfLCDVGDV 325

                          90
                  ....*....|....*..
gi 2205656896 327 EGMMSEALKIINNNEYY 343
Cdd:TIGR03999 326 ETMAEYAISLLEDEELL 342
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 12-367 8.64e-10

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.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 59.60  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  12 PAVSGATMIVTELLSRLPTKGVKVDLIELLFKEDEGllgrypelNEKVNVIDIIRIPYSGNLagRFIRYIYKNIILKRKI 91
Cdd:cd03817    11 PQVNGVATSVRNLARALEKRGHEVYVITPSDPGAED--------EEEVVRYRSFSIPIRKYH--RQHIPFPFKKAVIDRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  92 GNLidNYD-------FIIGINTAKSIRMLYLePFI-TFPL-YKHYLNliritNIIDGTAWFIDSVKGFRES--KRNKLNI 160
Cdd:cd03817    81 KEL--GPDiihthtpFSLGKLGLRIARKLKI-PIVhTYHTmYEDYLH-----YIPKGKLLVKAVVRKLVRRfyNHTDAVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 161 CLGSVLSKMVKtKYGIECEALDPPGGVDPNLVKDVTPF---------PENFDAIHLARQGFMKGTPEVIQIMKNLKKYGY 231
Cdd:cd03817   153 APSEKIKDTLR-EYGVKGPIEVIPNGIDLDKFEKPLNTeerrklglpPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 232 KKFAIIGGQDY-----GFDINKYLDDKdIVYFGEIlDKKRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLP 306
Cdd:cd03817   232 IKLVIVGDGPEreelkELARELGLADK-VIFTGFV-PREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDP 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205656896 307 AIRYYYGDCEAVKLVKEGDVEgmMSEAL-KIINNNEYYKSL---AFKCISKYTWDKVAESFVQIL 367
Cdd:cd03817   310 AASELVEDGENGFLFEPNDET--LAEKLlHLRENLELLRKLsknAEISAREFAFAKSVEKLYEEV 372
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 253-347 1.71e-09

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.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 58.90  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 253 KDIVYFGEILDKKRIYSIlksSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSE 332
Cdd:cd04962   252 DRVLFLGKQDDVEELLSI---ADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKS 328

                          90
                  ....*....|....*
gi 2205656896 333 ALKIINNNEYYKSLA 347
Cdd:cd04962   329 ALSILEDDELYNRMG 343
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 271-361 2.10e-09

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.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 58.55  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 271 LKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNN-------EYY 343
Cdd:cd03798   274 YRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAEPylrelgeAAR 353

                          90
                  ....*....|....*...
gi 2205656896 344 KSLAfkciSKYTWDKVAE 361
Cdd:cd03798   354 ARVA----ERFSWVKAAD 367
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 269-368 8.80e-09

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.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 56.53  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 269 SILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAF 348
Cdd:cd03814   263 RAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAA 342

                          90       100
                  ....*....|....*....|...
gi 2205656896 349 KC---ISKYTWDKVAESFVQILH 368
Cdd:cd03814   343 RAraeAERYSWEAFLDNLLDYYA 365
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 265-361 1.71e-08

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 55.71  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 265 KRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPairyyYGDCEAVK------LVKEGDVEGmMSEAL-KII 337
Cdd:cd03820   247 KNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCP-----TGPSEIIEdgenglLVPNGDVDA-LAEALlRLM 320

                          90       100
                  ....*....|....*....|....*..
gi 2205656896 338 NNNEYYKSL---AFKCISKYTWDKVAE 361
Cdd:cd03820   321 EDEELRKKMgknARKNAERFSIEKIIK 347
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 186-303 4.92e-08

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.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 54.22  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 186 GVDPNLVkDVTPFPENFdAIHLARQGFMKGTPEVIQIMKNLKKygykKFAIIGG---QDYGFDINKYLDDKDIVYFGEI- 261
Cdd:cd03802   156 GLDPADY-RFQPDPEDY-LAFLGRIAPEKGLEDAIRVARRAGL----PLKIAGKvrdEDYFYYLQEPLPGPRIEFIGEVg 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2205656896 262 LDKKRiySILKSSKIFIYPTHVD-SFGIVIAEALACGVPVIAY 303
Cdd:cd03802   230 HDEKQ--ELLGGARALLFPINWDePFGLVMIEAMACGTPVIAY 270
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 69-341 1.76e-07

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 52.36  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896  69 YSGNLAGRFIRYIYKNIILKRKIGNLIDNYDFI---IGINTAKSIRMlylePFITFplyKHylNLIRITNIIDGTAWFId 145
Cdd:cd03819    54 LKVPLLRALLGNVRLARLIRRERIDLIHAHSRApawLGWLASRLTGV----PLVTT---VH--GSYLATYHPKDFALAV- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 146 SVKGFR-----ESKRNKLNICLGSVLSKMVKTKYGIECEALDPPGGVDPNLVKDVtpfPENFDAI-HLARQGFMKGTPEV 219
Cdd:cd03819   124 RARGDRviavsELVRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAEERAQLGL---PEGKPVVgYVGRLSPEKGWLLL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 220 IQIMKNLKKYGYKKFAIIG-GQDYGFD---INKYLDDKDIVYFGEILDkkrIYSILKSSKIFIYPTHVDSFGIVIAEALA 295
Cdd:cd03819   201 VDAAAELKDEPDFRLLVAGdGPERDEIrrlVERLGLRDRVTFTGFRED---VPAALAASDVVVLPSLHEEFGRVALEAMA 277

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2205656896 296 CGVPVIAYDLPAIRyyygdcEAVK------LVKEGDVEGMMSEALKIINNNE 341
Cdd:cd03819   278 CGTPVVATDVGGAR------EIVVhgrtglLVPPGDAEALADAIRAAKLLPE 323
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 270-361 1.94e-07

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 52.63  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 270 ILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFK 349
Cdd:cd03800   299 LYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRA 378

                          90
                  ....*....|....*.
gi 2205656896 350 CI----SKYTWDKVAE 361
Cdd:cd03800   379 GLerarAHYTWESVAD 394
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 184-367 2.26e-07

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 52.33  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 184 PGGVDPNLVKDVTPF----PENFdaIHLARQGFMKGTPEVIQIMKNLKKYGYKkFAIIGGQDygFDINKYLDDKDIVYFG 259
Cdd:cd03823   172 PNAVEPDLAPPPRRRpgteRLRF--GYIGRLTEEKGIDLLVEAFKRLPREDIE-LVIAGHGP--LSDERQIEGGRRIAFL 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 260 EILDKKRIYSILKSSKIFIYPTH-VDSFGIVIAEALACGVPVIAYDLPAIRyyygdcEAVK------LVKEGDVEGMMSE 332
Cdd:cd03823   247 GRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIA------ELIQpgvnglLFAPGDAEDLAAA 320

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2205656896 333 ALKIINNNEYYKSLAFKCISKYTWDKVAESFVQIL 367
Cdd:cd03823   321 MRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 250-368 2.65e-07

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 51.93  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 250 LDDKdIVYFGEILDkkrIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPAIRYYYGDCEAVkLVKEGDVEGM 329
Cdd:cd03807   245 LEDR-VHLLGERSD---VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTGF-LVPAGDPQAL 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2205656896 330 MSEALKIINNNEYYKSLAF----KCISKYTWDKVAESFVQILH 368
Cdd:cd03807   320 ADAIRALLEDPEKRARLGRaareRIANEFSIDAMVRRYETLYY 362
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 218-364 2.88e-06

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 48.88  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 218 EVIQIMKNLKKYGYKKFAIIGGQDYGFDINKYLDDK--DIVYFGEILDKKRIYSILKSSKIFIYP-----THVDSFGIVI 290
Cdd:cd03794   234 TLLEAAERLKRRPDIRFLFVGDGDEKERLKELAKARglDNVTFLGRVPKEEVPELLSAADVGLVPlkdnpANRGSSPSKL 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656896 291 AEALACGVPVIAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSL---AFKCI-SKYTWDKVAESFV 364
Cdd:cd03794   314 FEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMgenGRELAeEKFSREKLADRLL 391
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 232-304 9.02e-06

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 47.28  E-value: 9.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205656896 232 KKFAIIGGqdyGFDINKYLD-DKDIVYFGEILDKKRIYSILKSSKIFIYPTHVDsFGIVIAEALACGVPVIAYD 304
Cdd:cd03804   226 KRLVVIGD---GPDLDRLRAmASPNVEFLGYQPDEVLKELLSKARAFVFAAEED-FGIVPVEAQACGTPVIAFG 295
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 253-347 1.34e-05

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.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 46.50  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 253 KDIVYFGEILDKKRiYSILKSSKIFIYPTHVDS--FGIVIAEALACGVPVIAYDLP-AIRYYYGDCEAVKLVKEGDVEGM 329
Cdd:cd03795   242 DNVKFLGRVDDEEK-VIYLHLCDVFVFPSVLRSeaFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDAL 320

                          90
                  ....*....|....*...
gi 2205656896 330 MSEALKIINNNEYYKSLA 347
Cdd:cd03795   321 AEAIDKLLSDEELRESYG 338
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 183-341 2.07e-05

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.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 46.14  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 183 PPGGVDPNLVKDVTPFPENFDAIHLARQGFMKGTPEVIQIMKNLKKYGYK-KFAIIGgqdYGFDINKYLDDKDIVYFGE- 260
Cdd:cd04949   142 PVGYVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEiTLDIYG---YGEEREKLKKLIEELHLEDn 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 261 -ILDK--KRIYSILKSSKIFIYPTHVDSFGIVIAEALACGVPVIAYDLPairyyYGDCEAVK------LVKEGDVEGMMS 331
Cdd:cd04949   219 vFLKGyhSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVK-----YGPSELIEdgengyLIEKNNIDALAD 293

                         170
                  ....*....|
gi 2205656896 332 EALKIINNNE 341
Cdd:cd04949   294 KIIELLNDPE 303
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 199-356 3.01e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.86  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 199 PENFDAIHLARQGFMKGTPEVIQIMKNLKKygyKKFAIIGGQDYGFDINKYLDDKDIVYFGeILDKKRIYSILKSSKIFI 278
Cdd:PLN02871  261 PEKPLIVYVGRLGAEKNLDFLKRVMERLPG---ARLAFVGDGPYREELEKMFAGTPTVFTG-MLQGDELSQAYASGDVFV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 279 YPTHVDSFGIVIAEALACGVPVIAY---DLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNEYYKSLAFKC---IS 352
Cdd:PLN02871  337 MPSESETLGFVVLEAMASGVPVVAAragGIPDIIPPDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAreeVE 416


                  ....
gi 2205656896 353 KYTW 356
Cdd:PLN02871  417 KWDW 420
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 252-368 2.98e-04

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 42.37  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 252 DKDIVYFGEILDKKRIYSILKSSKIFIYP---THVDSFGiVIAEALACGVPVIAYDLPAIRYYYGDCEAVkLVKEGDVEG 328
Cdd:cd03822   250 QDHVDFHNNFLPEEEVPRYISAADVVVLPylnTEQSSSG-TLSYAIACGKPVISTPLRHAEELLADGRGV-LVPFDDPSA 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2205656896 329 MMSEALKIINNNEY---YKSLAFKCISKYTWDKVAESFVQILH 368
Cdd:cd03822   328 IAEAILRLLEDDERrqaIAERAYAYARAMTWESIADRYLRLFN 370
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 222-348 4.37e-04

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.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 42.05  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 222 IMKNLKKYGYKKFAIIGGQDYGFDINKYLDD----KDIVYFGEILDKKRIYSilkSSKIFIYPTHVDSFGIVIAEALACG 297
Cdd:cd04951   210 ISELILSKNDFKLLIAGDGPLRNELERLICNlnlvDRVILLGQISNISEYYN---AADLFVLSSEWEGFGLVVAEAMACE 286

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2205656896 298 VPVIAYDLPAIRYYYGDCEAVKLV--------KEGDVEGMMSEALKIINNNEYYKSLAF 348
Cdd:cd04951   287 RPVVATDAGGVAEVVGDHNYVVPVsdpqllaeKIKEIFDMSDEERDILGNKNEYIAKNF 345
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 160-341 6.96e-03

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.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 38.20  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 160 ICLGSVLSKMVKTKYGIECEAL------DPPGGvdpnlvkdvtpfpenfdAIHLARQGFM---KGTPEVIQ-IMKNLKKY 229
Cdd:cd03799   141 IALGCDEKKIIVHRSGIDCNKFrfkpryLPLDG-----------------KIRILTVGRLtekKGLEYAIEaVAKLAQKY 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656896 230 GYKKFAIIGGQDYGFDINKYLDDKDIVYFGEIL---DKKRIYSILKSSKIFIYPTHV----DSFGIVIA--EALACGVPV 300
Cdd:cd03799   204 PNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLgwkPQEEIIEILDEADIFIAPSVTaadgDQDGPPNTlkEAMAMGLPV 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2205656896 301 IAYDLPAIRYYYGDCEAVKLVKEGDVEGMMSEALKIINNNE 341
Cdd:cd03799   284 ISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHPA 324
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH