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Conserved domains on  [gi|15597435|ref|NP_250929|]
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biofilm formation protein PslI [Pseudomonas aeruginosa PAO1]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133545)

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
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
2-361 1.16e-77

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: 243.04  E-value: 1.16e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   2 RIGLDYRTVGSsPHSGISRQVYAMEQALESLPGtQVTRFTVAPLDDPLRQRAVCPPW---GCPRTAMHQPHQRLRFEAGF 78
Cdd:cd03809   1 KILIDGRSLAQ-RLTGIGRYTRELLKALAKNDP-DESVLAVPPLPGELLRLLREYPElslGVIKIKLWRELALLRWLQIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  79 LPRALReqdIDLYISTFNmglPLPPRPPGVRYALLIHDLFQITLKNYHANRlkalvYRVSDYLSIAYALRVADRVWTPSQ 158
Cdd:cd03809  79 LPKKDK---PDLLHSPHN---TAPLLLKGCPQVVTIHDLIPLRYPEFFPKR-----FRLYYRLLLPISLRRADAIITVSE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 159 YSADEAVRLFPGVAGKVRVLPNQVDGFAGEPAD----LSARGLPPRYWLLVGTRELRKNVPWFVSAWTRARAQAPgVPPL 234
Cdd:cd03809 148 ATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESaavlIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLKL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 235 VLVGSLDHLPEE------QRGLPG-LHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDE 307
Cdd:cd03809 227 VIVGGKGWEDEElldlvkKLGLGGrVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597435 308 VTPPSAPRFSPSDGAALERLMLRLADAP--REASAEELIAWAARFNREAYRQRLAA 361
Cdd:cd03809 307 VAGDAALYFDPLDPESIADAILRLLEDPslREELIRKGLERAKKFSWEKTAEKTLE 362
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
2-361 1.16e-77

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: 243.04  E-value: 1.16e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   2 RIGLDYRTVGSsPHSGISRQVYAMEQALESLPGtQVTRFTVAPLDDPLRQRAVCPPW---GCPRTAMHQPHQRLRFEAGF 78
Cdd:cd03809   1 KILIDGRSLAQ-RLTGIGRYTRELLKALAKNDP-DESVLAVPPLPGELLRLLREYPElslGVIKIKLWRELALLRWLQIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  79 LPRALReqdIDLYISTFNmglPLPPRPPGVRYALLIHDLFQITLKNYHANRlkalvYRVSDYLSIAYALRVADRVWTPSQ 158
Cdd:cd03809  79 LPKKDK---PDLLHSPHN---TAPLLLKGCPQVVTIHDLIPLRYPEFFPKR-----FRLYYRLLLPISLRRADAIITVSE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 159 YSADEAVRLFPGVAGKVRVLPNQVDGFAGEPAD----LSARGLPPRYWLLVGTRELRKNVPWFVSAWTRARAQAPgVPPL 234
Cdd:cd03809 148 ATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESaavlIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLKL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 235 VLVGSLDHLPEE------QRGLPG-LHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDE 307
Cdd:cd03809 227 VIVGGKGWEDEElldlvkKLGLGGrVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597435 308 VTPPSAPRFSPSDGAALERLMLRLADAP--REASAEELIAWAARFNREAYRQRLAA 361
Cdd:cd03809 307 VAGDAALYFDPLDPESIADAILRLLEDPslREELIRKGLERAKKFSWEKTAEKTLE 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
203-310 2.83e-12

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: 64.22  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   203 LLVGTRELRKNVPWFVSAWTRARAQAPGVPpLVLVGSLDHLPE-----EQRGLPG-LHALGGLDDAELHALYRQAERLWQ 276
Cdd:pfam00534   6 LFVGRLEPEKGLDLLIKAFALLKEKNPNLK-LVIAGDGEEEKRlkklaEKLGLGDnVIFLGFVSDEDLPELLKIADVFVL 84
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15597435   277 PSYAEGFGLPVVEALSVGTPV-AVASGTSLDEVTP 310
Cdd:pfam00534  85 PSRYEGFGIVLLEAMACGLPViASDVGGPPEVVKD 119
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
258-366 1.56e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.16  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 258 GLDDAeLHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDEVTPP--SAPRFSPSDGAALERLMLRLADAP 335
Cdd:COG0438   9 GLDLL-LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDgeTGLLVPPGDPEALAEAILRLLEDP 87
                        90       100       110
                ....*....|....*....|....*....|....
gi 15597435 336 ---REASAEELIAWAARFNREAYRQRLAALIEEL 366
Cdd:COG0438  88 elrRRLGEAARERAEERFSWEAIAERLLALYEEL 121
mycothiol_MshA TIGR03449
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ...
150-365 1.79e-06

D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.


Pssm-ID: 132490 [Multi-domain]  Cd Length: 405  Bit Score: 49.35  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   150 ADRVWTPSQYSADEAVRLFPGVAGKVRVLPNQVDGFAGEPAD----LSARGLPPRYWLL--VGTRELRKNVPWFVSAWTR 223
Cdd:TIGR03449 164 ADRLIANTDEEARDLVRHYDADPDRIDVVAPGADLERFRPGDrateRARLGLPLDTKVVafVGRIQPLKAPDVLLRAVAE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   224 ARAQAPGVPPLVLV-----GSLDHLPEeqrGLPGLHALGGLDD----------AELHALYRQAERLWQPSYAEGFGLPVV 288
Cdd:TIGR03449 244 LLDRDPDRNLRVIVvggpsGSGLATPD---ALIELAAELGIADrvrflpprppEELVHVYRAADVVAVPSYNESFGLVAM 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   289 EALSVGTPVAVASGTSL-----DEVTPPSAPRFSPSDGA-ALERLMlrLADAPREASAEELIAWAARFNREAYRQRLAAL 362
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLpvavaDGETGLLVDGHDPADWAdALARLL--DDPRTRIRMGAAAVEHAAGFSWAATADGLLSS 398

                  ...
gi 15597435   363 IEE 365
Cdd:TIGR03449 399 YRD 401
PHA01630 PHA01630
putative group 1 glycosyl transferase
131-365 7.50e-05

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 44.01  E-value: 7.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  131 KALVYRVSDYLSIAY-ALRVADRVWT-----PSQYSADEAVRLFPGVAGKVRVLPNQVDG--FAGEPADLSAR---GLPP 199
Cdd:PHA01630  70 KNIVFEVADTDAISHtALYFFRNQPVdeivvPSQWSKNAFYTSGLKIPQPIYVIPHNLNPrmFEYKPKEKPHPcvlAILP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  200 RYWLlvgtrelRKNVPWFVSAWTRARAQAPGVPPLVLvgSLDHLPEEQRGLPGLHAlgGLDDAELHALYRQAERLWQPSY 279
Cdd:PHA01630 150 HSWD-------RKGGDIVVKIFHELQNEGYDFYFLIK--SSNMLDPRLFGLNGVKT--PLPDDDIYSLFAGCDILFYPVR 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  280 AEGFGLPVVEALSVGTPVAVASGTSLDEVTPPS----------APRFSPSD------------GAALERLMLRLADAPRE 337
Cdd:PHA01630 219 GGAFEIPVIEALALGLDVVVTEKGAWSEWVLSNldvywiksgrKPKLWYTNpihvgyfldpdiEDAYQKLLEALANWTPE 298
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15597435  338 ASAEEL----IAWAARFNREAYRQRLAALIEE 365
Cdd:PHA01630 299 KKKENLegraILYRENYSYNAIAKMWEKILEK 330
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
2-361 1.16e-77

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: 243.04  E-value: 1.16e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   2 RIGLDYRTVGSsPHSGISRQVYAMEQALESLPGtQVTRFTVAPLDDPLRQRAVCPPW---GCPRTAMHQPHQRLRFEAGF 78
Cdd:cd03809   1 KILIDGRSLAQ-RLTGIGRYTRELLKALAKNDP-DESVLAVPPLPGELLRLLREYPElslGVIKIKLWRELALLRWLQIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  79 LPRALReqdIDLYISTFNmglPLPPRPPGVRYALLIHDLFQITLKNYHANRlkalvYRVSDYLSIAYALRVADRVWTPSQ 158
Cdd:cd03809  79 LPKKDK---PDLLHSPHN---TAPLLLKGCPQVVTIHDLIPLRYPEFFPKR-----FRLYYRLLLPISLRRADAIITVSE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 159 YSADEAVRLFPGVAGKVRVLPNQVDGFAGEPAD----LSARGLPPRYWLLVGTRELRKNVPWFVSAWTRARAQAPgVPPL 234
Cdd:cd03809 148 ATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESaavlIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLKL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 235 VLVGSLDHLPEE------QRGLPG-LHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDE 307
Cdd:cd03809 227 VIVGGKGWEDEElldlvkKLGLGGrVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597435 308 VTPPSAPRFSPSDGAALERLMLRLADAP--REASAEELIAWAARFNREAYRQRLAA 361
Cdd:cd03809 307 VAGDAALYFDPLDPESIADAILRLLEDPslREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
14-364 1.17e-22

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: 97.61  E-value: 1.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  14 PHSGISRQVYAMEQALESLpGTQVTRFTVAPLDDPL-RQRAVCPPWGCPRTAMHQPHQRLRFEAGFLPRALREQDIDLYI 92
Cdd:cd03801  12 PVGGAERHVRELARALAAR-GHDVTVLTPADPGEPPeELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  93 STFNMGLPLPPRPPGVRYALLIHDLFQITLKNYHANRLKALVYrvsdylsIAYALRVADRVWTPSQYSADEAVRLFPGVA 172
Cdd:cd03801  91 LLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLAR-------AEALLRRADAVIAVSEALRDELRALGGIPP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 173 GKVRVLPNQVDGFAGEPADLSARGLPP--RYWLLVGTRELRKNVPWFVSAWTRARAQAPGVPpLVLVGS----LDHLPEE 246
Cdd:cd03801 164 EKIVVIPNGVDLERFSPPLRRKLGIPPdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVR-LVIVGGdgplRAELEEL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 247 QRGL-PGLHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDEVTPPSAPRF--SPSDGAA 323
Cdd:cd03801 243 ELGLgDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLvvPPDDVEA 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15597435 324 LERLMLRLADAP---REASAEELIAWAARFNREAYRQRLAALIE 364
Cdd:cd03801 323 LADALLRLLADPelrARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
143-362 5.62e-15

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: 75.49  E-value: 5.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 143 IAYALRVADRVWTPSQYSADEAVRLFPgVAGKVRVLPNQVDGFAGEPADLSAR-GLPPRYWLLVGTRELRKNVPWFVSAW 221
Cdd:cd03798 144 LRWALRRAARVIAVSKALAEELVALGV-PRDRVDVIPNGVDPARFQPEDRGLGlPLDAFVILFVGRLIPRKGIDLLLEAF 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 222 TRARAQAPGVPpLVLVGS------LDHLPEEQRGLPGLHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGT 295
Cdd:cd03798 223 ARLAKARPDVV-LLIVGDgplreaLRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGL 301
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597435 296 PV-AVASGTSLDEVTPPSA-----PRFSPSDGAALERLmlrLADAPREASAEELIA-WAARFNREAYRQRLAAL 362
Cdd:cd03798 302 PVvATDVGGIPEVVGDPETgllvpPGDADALAAALRRA---LAEPYLRELGEAARArVAERFSWVKAADRIAAA 372
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
155-339 7.92e-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: 71.98  E-value: 7.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 155 TPSQYSADEAVRLFPGVAGKVRVLPNQVDGFAGEPADL----SARGLP-PRYWLLVGTR---ELRKNVPWFVsawtRARA 226
Cdd:cd03825 143 APSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDKakarKRLGIPqDKKVILFGAEsvtKPRKGFDELI----EALK 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 227 QAPGVPPLVLVgSLDHLPEEQRGLPG-LHALGGL-DDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPV-AVASGT 303
Cdd:cd03825 219 LLATKDDLLLV-VFGKNDPQIVILPFdIISLGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVvAFDTGG 297
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15597435 304 SLDEVTPPS----APRFSPSDGA-ALERL------MLRLADAPREAS 339
Cdd:cd03825 298 SPEIVQHGVtgylVPPGDVQALAeAIEWLlanpkeRESLGERARALA 344
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
146-355 1.60e-12

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: 68.16  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 146 ALRVADRVWTPSQYSADEAvrLFPGVAGKVRVLPNQVD--GFAGEPADLSARGLPP--RYWLLVGTRELRKNVPWFVSAW 221
Cdd:cd03821 149 NLNNAALVHFTSEQEADEL--RRFGLEPPIAVIPNGVDipEFDPGLRDRRKHNGLEdrRIILFLGRIHPKKGLDLLIRAA 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 222 TRARAQAPGVPpLVLVGSLDHLPEEQRGL-------PGLHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVG 294
Cdd:cd03821 227 RKLAEQGRDWH-LVIAGPDDGAYPAFLQLqsslglgDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACG 305
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597435 295 TPVAVASGTSLDEVTPPSAPRFSPSDGAALERLMLRLADAPREASAEELIAWAARFNREAY 355
Cdd:cd03821 306 LPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQVEENF 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
203-310 2.83e-12

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: 64.22  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   203 LLVGTRELRKNVPWFVSAWTRARAQAPGVPpLVLVGSLDHLPE-----EQRGLPG-LHALGGLDDAELHALYRQAERLWQ 276
Cdd:pfam00534   6 LFVGRLEPEKGLDLLIKAFALLKEKNPNLK-LVIAGDGEEEKRlkklaEKLGLGDnVIFLGFVSDEDLPELLKIADVFVL 84
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15597435   277 PSYAEGFGLPVVEALSVGTPV-AVASGTSLDEVTP 310
Cdd:pfam00534  85 PSRYEGFGIVLLEAMACGLPViASDVGGPPEVVKD 119
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
150-366 7.13e-12

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: 65.78  E-value: 7.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 150 ADRVWTPSQYSADEAVRLfpgVAGKVRVLPNQVDG--F---AGEPADLSARGLPPRYWLL-VGTRELRKNVPWFVSAWTR 223
Cdd:cd03814 146 FDTTLVPSPSIARELEGH---GFERVRLWPRGVDTelFhpsRRDAALRRRLGPPGRPLLLyVGRLAPEKNLEALLDADLP 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 224 ARAQAPgvPPLVLVGSLDHLPEEQRGLPGLHALGGLDDAELHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVA-SG 302
Cdd:cd03814 223 LAASPP--VRLVVVGDGPARAELEARGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAAdAG 300
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597435 303 TSLDEVTPPSAPR-FSPSDGAALERLMLRLAdapreASAEELIAWAARFNREAYRQRLAALIEEL 366
Cdd:cd03814 301 GPRDIVRPGGTGAlVEPGDAAAFAAALRALL-----EDPELRRRMAARARAEAERYSWEAFLDNL 360
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
125-366 1.06e-11

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: 65.38  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 125 YHANRLKALVYRVSDYLSIAYaLRVADRVWTPSQYSADEAVRLfpGVAGKVRVLPNQVD----GFAGEPADLSARGLPPR 200
Cdd:cd03817 124 HYIPKGKLLVKAVVRKLVRRF-YNHTDAVIAPSEKIKDTLREY--GVKGPIEVIPNGIDldkfEKPLNTEERRKLGLPPD 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 201 YWLL--VG--TRElrKNVpwfvSAWTRARAQAPGVPP--LVLVG------SLDHLPEEQRGLPGLHALGGLDDAELHALY 268
Cdd:cd03817 201 EPILlyVGrlAKE--KNI----DFLLRAFAELKKEPNikLVIVGdgpereELKELARELGLADKVIFTGFVPREELPEYY 274
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 269 RQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDEV---------TPPSAPRFSpsdgAALERLMLRLADAPREAS 339
Cdd:cd03817 275 KAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELvedgengflFEPNDETLA----EKLLHLRENLELLRKLSK 350
                       250       260
                ....*....|....*....|....*..
gi 15597435 340 AEELIAWAARFNReayrqRLAALIEEL 366
Cdd:cd03817 351 NAEISAREFAFAK-----SVEKLYEEV 372
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
258-366 1.56e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 61.16  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 258 GLDDAeLHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVAVASGTSLDEVTPP--SAPRFSPSDGAALERLMLRLADAP 335
Cdd:COG0438   9 GLDLL-LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDgeTGLLVPPGDPEALAEAILRLLEDP 87
                        90       100       110
                ....*....|....*....|....*....|....
gi 15597435 336 ---REASAEELIAWAARFNREAYRQRLAALIEEL 366
Cdd:COG0438  88 elrRRLGEAARERAEERFSWEAIAERLLALYEEL 121
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
151-364 8.36e-10

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: 59.65  E-value: 8.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 151 DRVWTPSQYSADEAVRLFPGVAgKVRVLPNQVDGFAGEPADLSARGLPPRYwLLVGTRELRKNVPWFVSAWTRAraqAPG 230
Cdd:cd03823 145 DAVLAPSRFTANLHEANGLFSA-RISVIPNAVEPDLAPPPRRRPGTERLRF-GYIGRLTEEKGIDLLVEAFKRL---PRE 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 231 VPPLVLVGS-LDHLPEEQRGLPGLHALGGLDDAELHALYRQAERLWQPS-YAEGFGLPVVEALSVGTPVAVASGTSLDEV 308
Cdd:cd03823 220 DIELVIAGHgPLSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAGLPVIASDLGGIAEL 299
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597435 309 TPPSAP--RFSPSDGAALERLMLRLADAPreaSAEELIAWAARfNREAYRQRLAALIE 364
Cdd:cd03823 300 IQPGVNglLFAPGDAEDLAAAMRRLLTDP---ALLERLRAGAE-PPRSTESQAEEYLK 353
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-301 1.12e-09

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 55.98  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   211 RKNVPWFVSAWTRARAQAPGVPpLVLVGS--LDHLPEEQRGLP-GLHALGGLDDaeLHALYRQAERLWQPSYAEGFGLPV 287
Cdd:pfam13692  14 VKGVDYLLEAVPLLRKRDNDVR-LVIVGDgpEEELEELAAGLEdRVIFTGFVED--LAELLAAADVFVLPSLYEGFGLKL 90
                          90
                  ....*....|....
gi 15597435   288 VEALSVGTPVaVAS 301
Cdd:pfam13692  91 LEAMAAGLPV-VAT 103
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
194-308 1.20e-08

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: 55.10  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 194 ARGLPPRYWLLVGTRELRKNVPWFVSAWTRARAQAPGVPpLVLVGSLDHLPEEQ------RGLPGLHALGGLDDAELHAL 267
Cdd:cd01635 105 LVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLV-LVLVGGGGEREEEEalaaalGLLERVVIIGGLVDDEVLEL 183
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15597435 268 YRQAERLW-QPSYAEGFGLPVVEALSVGTPVAVASGTSLDEV 308
Cdd:cd01635 184 LLAAADVFvLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEF 225
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
143-308 1.16e-07

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: 53.12  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 143 IAYALRVADRVWTPSQYSADEAVRLFPgVAGKVRVLPNQVDG--FAGEPAD--LSARGLPPRYWLLVGTRELR--KNVPW 216
Cdd:cd04962 135 VRFSINKSDRVTAVSSSLRQETYELFD-VDKDIEVIHNFIDEdvFKRKPAGalKRRLLAPPDEKVVIHVSNFRpvKRIDD 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 217 FVSAWTRARAQAPGvpPLVLVGSLdhlPEEQRGLPGLHALGGLDDA-------ELHALYRQAERLWQPSYAEGFGLPVVE 289
Cdd:cd04962 214 VVRVFARVRRKIPA--KLLLVGDG---PERVPAEELARELGVEDRVlflgkqdDVEELLSIADLFLLPSEKESFGLAALE 288
                       170
                ....*....|....*....
gi 15597435 290 ALSVGTPVAVASGTSLDEV 308
Cdd:cd04962 289 AMACGVPVVSSNAGGIPEV 307
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
127-358 1.50e-07

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: 52.60  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 127 ANRLKALVYRVSDYLsiayALRVADRVWTPSQYSADEAVRL-FPGVAGKVRVLPNQVDGFAGEPADLSARGLPPRYwLLV 205
Cdd:cd03808 121 EGKLLRLLYLLLEKL----ALLFTDKVIFVNEDDRDLAIKKgIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVF-LFV 195
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 206 GtRELR-KNVPWFVSAWTRARAQAPGVPpLVLVGSLDHLPE-----EQRGLPGL-HALGGLDDAElhALYRQAERLWQPS 278
Cdd:cd03808 196 A-RLLKdKGIDELIEAAKILKKKGPNVR-FLLVGDGELENPseiliEKLGLEGRiEFLGFRSDVP--ELLAESDVFVLPS 271
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 279 YAEGFGLPVVEALSVGTPVaVAS---GTS---LDEVTPPSAPrfsPSDGAALERLMLRLADAPreasaeELIAWAARFNR 352
Cdd:cd03808 272 YREGLPRSLLEAMAAGRPV-ITTdvpGCRelvIDGVNGFLVP---PGDVEALADAIEKLIEDP------ELRKEMGEAAR 341

                ....*.
gi 15597435 353 EAYRQR 358
Cdd:cd03808 342 KRVEEK 347
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
146-300 4.74e-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: 51.09  E-value: 4.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 146 ALRVADRVWTPSQYSADEAVRLFPGVAGKVRVLPNQVD-----GFAGEPADLSARGLPP--RYWLLVGTRELRKNVPWFV 218
Cdd:cd03800 160 ILEAADRVIASTPQEADELISLYGADPSRINVVPPGVDlerffPVDRAEARRARLLLPPdkPVVLALGRLDPRKGIDTLV 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 219 SAWTRARAQAPGVPPLVLVGSLDHL----PEEQRGLPGLHAL-------GGLDDAELHALYRQAERLWQPSYAEGFGLPV 287
Cdd:cd03800 240 RAFAQLPELRELANLVLVGGPSDDPlsmdREELAELAEELGLidrvrfpGRVSRDDLPELYRAADVFVVPSLYEPFGLTA 319
                       170
                ....*....|...
gi 15597435 288 VEALSVGTPVAVA 300
Cdd:cd03800 320 IEAMACGTPVVAT 332
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
150-356 1.60e-06

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: 49.28  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 150 ADRVWTPSQYSADEAVRLFPGVAGKVRVLPNQVD----GFAGEPADLSARGLPPRYW--LLVG--TRElrKNVPWFVsaw 221
Cdd:cd03819 127 GDRVIAVSELVRDHLIEALGVDPERIRVIPNGVDtdrfPPEAEAEERAQLGLPEGKPvvGYVGrlSPE--KGWLLLV--- 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 222 tRARAQAPGVPPLVLV----GSLDHLPEEQRGLPGL----HALGGLDDaeLHALYRQAERLWQPSYAEGFGLPVVEALSV 293
Cdd:cd03819 202 -DAAAELKDEPDFRLLvagdGPERDEIRRLVERLGLrdrvTFTGFRED--VPAALAASDVVVLPSLHEEFGRVALEAMAC 278
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597435 294 GTPV-AVASGTSLDEVTPPSAPRFS-PSDGAALERLMLRLADAPREASAEEliawAARFNREAYR 356
Cdd:cd03819 279 GTPVvATDVGGAREIVVHGRTGLLVpPGDAEALADAIRAAKLLPEAREKLQ----AAAALTEAVR 339
mycothiol_MshA TIGR03449
D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively ...
150-365 1.79e-06

D-inositol-3-phosphate glycosyltransferase; Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.


Pssm-ID: 132490 [Multi-domain]  Cd Length: 405  Bit Score: 49.35  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   150 ADRVWTPSQYSADEAVRLFPGVAGKVRVLPNQVDGFAGEPAD----LSARGLPPRYWLL--VGTRELRKNVPWFVSAWTR 223
Cdd:TIGR03449 164 ADRLIANTDEEARDLVRHYDADPDRIDVVAPGADLERFRPGDrateRARLGLPLDTKVVafVGRIQPLKAPDVLLRAVAE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   224 ARAQAPGVPPLVLV-----GSLDHLPEeqrGLPGLHALGGLDD----------AELHALYRQAERLWQPSYAEGFGLPVV 288
Cdd:TIGR03449 244 LLDRDPDRNLRVIVvggpsGSGLATPD---ALIELAAELGIADrvrflpprppEELVHVYRAADVVAVPSYNESFGLVAM 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435   289 EALSVGTPVAVASGTSL-----DEVTPPSAPRFSPSDGA-ALERLMlrLADAPREASAEELIAWAARFNREAYRQRLAAL 362
Cdd:TIGR03449 321 EAQACGTPVVAARVGGLpvavaDGETGLLVDGHDPADWAdALARLL--DDPRTRIRMGAAAVEHAAGFSWAATADGLLSS 398

                  ...
gi 15597435   363 IEE 365
Cdd:TIGR03449 399 YRD 401
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
172-366 1.90e-06

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.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 49.37  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 172 AGKVRVLPNQVDGFAGEPADlsaRGLPPRYWLLVGTRELRKNVPWFVSAWTRARAQAPgVPPLVLVGSLDHLPEEQ---R 248
Cdd:cd05844 165 AERIHVHYIGIDPAKFAPRD---PAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHP-TARLVIAGDGPLRPALQalaA 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 249 GLPGLHALGGLDDAELHALYRQAERLWQPSY------AEGFGLPVVEALSVGTPVAVASGTSLDEVTP--PSAPRFSPSD 320
Cdd:cd05844 241 ALGRVRFLGALPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILdgETGFLVPEGD 320
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15597435 321 GAAL-ERLMLRLADaprEASAEELIAWAARFNREAYRQRLAALIEEL 366
Cdd:cd05844 321 VDALaDALQALLAD---RALADRMGGAARAFVCEQFDIRVQTAKLEA 364
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
174-366 3.37e-05

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: 45.39  E-value: 3.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 174 KVRVLPNQVDGFAGEPADLSARGLPPRYWL--------LVGTRELRKNVPWFVSAWTRARAQAPGVPpLVLVGS--LDHL 243
Cdd:cd03807 157 KIVVIYNGIDLFKLSPDDASRARARRRLGLaedrrvigIVGRLHPVKDHSDLLRAAALLVETHPDLR-LLLVGRgpERPN 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 244 PEEQR---GLPG-LHALGGLDDaeLHALYRQAERLWQPSYAEGFGLPVVEALSVGTPVaVAS--GTSLDEVTPPSAPRFS 317
Cdd:cd03807 236 LERLLlelGLEDrVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPV-VATdvGGAAELVDDGTGFLVP 312
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15597435 318 PSDGAALERLMLRLADAPrEASAEELIAWAARFNREAYRQRLAALIEEL 366
Cdd:cd03807 313 AGDPQALADAIRALLEDP-EKRARLGRAARERIANEFSIDAMVRRYETL 360
PHA01630 PHA01630
putative group 1 glycosyl transferase
131-365 7.50e-05

putative group 1 glycosyl transferase


Pssm-ID: 164861  Cd Length: 331  Bit Score: 44.01  E-value: 7.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  131 KALVYRVSDYLSIAY-ALRVADRVWT-----PSQYSADEAVRLFPGVAGKVRVLPNQVDG--FAGEPADLSAR---GLPP 199
Cdd:PHA01630  70 KNIVFEVADTDAISHtALYFFRNQPVdeivvPSQWSKNAFYTSGLKIPQPIYVIPHNLNPrmFEYKPKEKPHPcvlAILP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  200 RYWLlvgtrelRKNVPWFVSAWTRARAQAPGVPPLVLvgSLDHLPEEQRGLPGLHAlgGLDDAELHALYRQAERLWQPSY 279
Cdd:PHA01630 150 HSWD-------RKGGDIVVKIFHELQNEGYDFYFLIK--SSNMLDPRLFGLNGVKT--PLPDDDIYSLFAGCDILFYPVR 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  280 AEGFGLPVVEALSVGTPVAVASGTSLDEVTPPS----------APRFSPSD------------GAALERLMLRLADAPRE 337
Cdd:PHA01630 219 GGAFEIPVIEALALGLDVVVTEKGAWSEWVLSNldvywiksgrKPKLWYTNpihvgyfldpdiEDAYQKLLEALANWTPE 298
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15597435  338 ASAEEL----IAWAARFNREAYRQRLAALIEE 365
Cdd:PHA01630 299 KKKENLegraILYRENYSYNAIAKMWEKILEK 330
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
226-366 2.33e-04

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: 42.66  E-value: 2.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 226 AQAPGVPpLVLVGSLDHLP-----EEQRGLPGLHALGGLDDAELHALYRQAERLWQPS-YAEGFGLPVVEALSVGTPVAV 299
Cdd:cd03802 191 ARRAGLP-LKIAGKVRDEDyfyylQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPInWDEPFGLVMIEAMACGTPVIA 269
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597435 300 ASGTSLDEVTPPSAPRFSPSDGAALERLMLRLADAPREASAEeliaWA-ARFNREAYRQRLAALIEEL 366
Cdd:cd03802 270 YRRGGLPEVIQHGETGFLVDSVEEMAEAIANIDRIDRAACRR----YAeDRFSAARMADRYEALYRKV 333
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-183 3.75e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 40.59  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435    17 GISRQVYAMEQALESLpGTQVTRFTVAPLDDPLRQRAVCPPWGCPRTAMHQPHQRLRFEAGFLPRALREQDIDLYISTFN 96
Cdd:pfam13439   2 GVERYVLELARALARR-GHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435    97 MGLPLPPRPPGVRYALLI----HDLFQITLKNYHANRLKALVYRvsdyLSIAYALRVADRVWTPSQYSADEAVRLFPGVA 172
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLvvtyHGLFPDYKRLGARLSPLRRLLR----RLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
                         170
                  ....*....|.
gi 15597435   173 GKVRVLPNQVD 183
Cdd:pfam13439 157 EKIRVIPNGVD 167
PHA01633 PHA01633
putative glycosyl transferase group 1
211-309 4.99e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 41.50  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435  211 RKNVPWFVSAWTRARAQAPGVPPLVLVGSLDHLPEEQRGLPG-LH---ALGGLDDAELHALYRQAERLWQPSYAEGFGLP 286
Cdd:PHA01633 160 RKNMDLMLQVFNELNTKYPDIAKKIHFFVISHKQFTQLEVPAnVHfvaEFGHNSREYIFAFYGAMDFTIVPSGTEGFGMP 239
                         90       100
                 ....*....|....*....|...
gi 15597435  287 VVEALSVGTPVAVASGTSLDEVT 309
Cdd:PHA01633 240 VLESMAMGTPVIHQLMPPLDEFT 262
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
232-331 1.52e-03

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: 40.34  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 232 PPLVLVGS--LDHLPEEQRGLPGL---HALGGLDDAELHALYRQAERLWQPSY--AEGFGLPVVEALSVGTPV---AVAS 301
Cdd:cd03795 218 YPIVIGGEgpLKPDLEAQIELNLLdnvKFLGRVDDEEKVIYLHLCDVFVFPSVlrSEAFGIVLLEAMMCGKPVistNIGT 297
                        90       100       110
                ....*....|....*....|....*....|...
gi 15597435 302 GT---SLDEVTPPSAPrfsPSDGAALERLMLRL 331
Cdd:cd03795 298 GVpyvNNNGETGLVVP---PKDPDALAEAIDKL 327
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
233-359 7.62e-03

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: 38.03  E-value: 7.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597435 233 PLVLVGS---LDHLpeEQRGLPGLHALGGLDDAELHALYRQAERLWQPSyAEGFGLPVVEALSVGTPV-AVASGTSLDEV 308
Cdd:cd03804 227 RLVVIGDgpdLDRL--RAMASPNVEFLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPViAFGKGGALETV 303
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15597435 309 TP-PSAPRFSPSDGAALERLMLRLADAPREASAEELIAWAARFNREAYRQRL 359
Cdd:cd03804 304 RPgPTGILFGEQTVESLKAAVEEFEQNFDRFKPQAIRANAERFSRARFRQEI 355
 
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.
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