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Conserved domains on  [gi|2532411019|ref|WP_289917089|]
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MULTISPECIES: glycosyltransferase [unclassified Janthinobacterium]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 6-361 9.48e-68

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.


The actual alignment was detected with superfamily member cd03798:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 376  Bit Score: 218.02  E-value: 9.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   6 LGPGNSIHISRWCNAMVEQGIEVHLITQHDF-------------DALQYSDRVHVHMLPYRGGKGYFLNRRALGKVLA-- 70
Cdd:cd03798    12 NSPGRGIFVRRQVRALSRRGVDVEVLAPAPWgpaaarllrkllgEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKrr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  71 -DLAPDLLNCHYASGYGTLMAGVWRGS---SLLSVWGADVYEFPYESRFKMwLIKRNLLAATRIASTSHVMAEQTRSLCP 146
Cdd:cd03798    92 rRGPPDLIHAHFAYPAGFAAALLARLYgvpYVVTEHGSDINVFPPRSLLRK-LLRWALRRAARVIAVSKALAEELVALGV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 147 QLAPIFITPFGIDTTRFVPVQKTDDARL---VIGTVKTMARKYGIDILIKGYALLRQRLQAEKA----DDllgrlelllv 219
Cdd:cd03798   171 PRDRVDVIPNGVDPARFQPEDRGLGLPLdafVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLlivgDG---------- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 220 gggAETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVV 299
Cdd:cd03798   241 ---PLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532411019 300 AENETGLIIPNENPQALADALYQLVQDSALRtRLGVAGRARVCQQFSWEHCVTLMRDAYVQT 361
Cdd:cd03798   316 GDPETGLLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRIAAAYRDV 376
 
Name Accession Description Interval E-value
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 6-361 9.48e-68

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: 218.02  E-value: 9.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   6 LGPGNSIHISRWCNAMVEQGIEVHLITQHDF-------------DALQYSDRVHVHMLPYRGGKGYFLNRRALGKVLA-- 70
Cdd:cd03798    12 NSPGRGIFVRRQVRALSRRGVDVEVLAPAPWgpaaarllrkllgEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKrr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  71 -DLAPDLLNCHYASGYGTLMAGVWRGS---SLLSVWGADVYEFPYESRFKMwLIKRNLLAATRIASTSHVMAEQTRSLCP 146
Cdd:cd03798    92 rRGPPDLIHAHFAYPAGFAAALLARLYgvpYVVTEHGSDINVFPPRSLLRK-LLRWALRRAARVIAVSKALAEELVALGV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 147 QLAPIFITPFGIDTTRFVPVQKTDDARL---VIGTVKTMARKYGIDILIKGYALLRQRLQAEKA----DDllgrlelllv 219
Cdd:cd03798   171 PRDRVDVIPNGVDPARFQPEDRGLGLPLdafVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLlivgDG---------- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 220 gggAETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVV 299
Cdd:cd03798   241 ---PLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532411019 300 AENETGLIIPNENPQALADALYQLVQDSALRtRLGVAGRARVCQQFSWEHCVTLMRDAYVQT 361
Cdd:cd03798   316 GDPETGLLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRIAAAYRDV 376
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 173-340 1.71e-32

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: 119.30  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 173 RLVIGTVKTMARKYGIDILIKGYALLRQRLQAEK---ADDLlgrlelllvgggAETAALQALVEQLGLGASVTFTGQVDH 249
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKlviAGDG------------EEEKRLKKLAEKLGLGDNVIFLGFVSD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 250 AAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSAL 329
Cdd:pfam00534  70 EDLPELLKIADVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEEL 147

                         170
                  ....*....|.
gi 2532411019 330 RTRLGVAGRAR 340
Cdd:pfam00534 148 RERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 255-363 3.17e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 106.61  E-value: 3.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 255 WLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLG 334
Cdd:COG0438    17 LLAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLG 94

                          90       100
                  ....*....|....*....|....*....
gi 2532411019 335 VAGRARVCQQFSWEHCVTLMRDAYVQTLA 363
Cdd:COG0438    95 EAARERAEERFSWEAIAERLLALYEELLA 123
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 117-356 1.34e-12

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 68.58  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 117 MWLIKRNLLAATRIA-STSHVMAEQTRSLCPQLAP-IFITPFGIDTTRFVPVQKTDDARL----------VIGTV----- 179
Cdd:PLN02871  195 MWDIIRFLHRAADLTlVTSPALGKELEAAGVTAANrIRVWNKGVDSESFHPRFRSEEMRArlsggepekpLIVYVgrlga 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 180 --------KTMARKYGIDILIKGYALLRQRLqaekaddllgrlelllvgggaetaalqalvEQLGLGASVTFTGQVDHAA 251
Cdd:PLN02871  275 eknldflkRVMERLPGARLAFVGDGPYREEL------------------------------EKMFAGTPTVFTGMLQGDE 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 252 VPDWLNRLDIYVAASrnDSESFGVAILEASSCALPVVVSRMGGLPEVVA---ENETGLIIPnenPQALADA---LYQLVQ 325
Cdd:PLN02871  325 LSQAYASGDVFVMPS--ESETLGFVVLEAMASGVPVVAARAGGIPDIIPpdqEGKTGFLYT---PGDVDDCvekLETLLA 399

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2532411019 326 DSALRTRLGVAGRARVcQQFSWEHCVTLMRD 356
Cdd:PLN02871  400 DPELRERMGAAAREEV-EKWDWRAATRKLRN 429
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 231-352 1.63e-09

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


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 59.41  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  231 LVEQLGLGASVTFTGQVDHAAVPDwlnrldIYVAASRNDS--------ESFGVAILEASSCALPVVVSRMGGLPEVVAEN 302
Cdd:TIGR02468  540 LIDKYDLYGQVAYPKHHKQSDVPD------IYRLAAKTKGvfinpafiEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVL 613

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2532411019  303 ETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVcQQFSW-EHCVT 352
Cdd:TIGR02468  614 DNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNI-HLFSWpEHCKT 663
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 230-358 3.96e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 45.31  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 230 ALVEQLGLGASVTFTG--QVDhaavpDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMG-------GL-PEVV 299
Cdd:NF038011  358 SLVASLGLQDKVKFLGfqKID-----DLLPQVGLMVLSSI--SEALPLVVLEAFAAGVPVVTTDVGscrqlieGLdEEDR 430

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2532411019 300 AENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSwehcVTLMRDAY 358
Cdd:NF038011  431 ALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYT----EELMFDRY 485
 
Name Accession Description Interval E-value
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 6-361 9.48e-68

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: 218.02  E-value: 9.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   6 LGPGNSIHISRWCNAMVEQGIEVHLITQHDF-------------DALQYSDRVHVHMLPYRGGKGYFLNRRALGKVLA-- 70
Cdd:cd03798    12 NSPGRGIFVRRQVRALSRRGVDVEVLAPAPWgpaaarllrkllgEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKrr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  71 -DLAPDLLNCHYASGYGTLMAGVWRGS---SLLSVWGADVYEFPYESRFKMwLIKRNLLAATRIASTSHVMAEQTRSLCP 146
Cdd:cd03798    92 rRGPPDLIHAHFAYPAGFAAALLARLYgvpYVVTEHGSDINVFPPRSLLRK-LLRWALRRAARVIAVSKALAEELVALGV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 147 QLAPIFITPFGIDTTRFVPVQKTDDARL---VIGTVKTMARKYGIDILIKGYALLRQRLQAEKA----DDllgrlelllv 219
Cdd:cd03798   171 PRDRVDVIPNGVDPARFQPEDRGLGLPLdafVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLlivgDG---------- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 220 gggAETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVV 299
Cdd:cd03798   241 ---PLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSR--HEGFGLVLLEAMACGLPVVATDVGGIPEVV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532411019 300 AENETGLIIPNENPQALADALYQLVQDSALRtRLGVAGRARVCQQFSWEHCVTLMRDAYVQT 361
Cdd:cd03798   316 GDPETGLLVPPGDADALAAALRRALAEPYLR-ELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-358 2.97e-54

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: 182.74  E-value: 2.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   2 KIAILGP-------GNSIHISRWCNAMVEQGIEVHLITQHDFDALQYSDRVHVHMLPYRGGKGYFLNRRALGKV---LAD 71
Cdd:cd03801     1 KILLLSPelpppvgGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELrplLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  72 LAPDLLNCH--YASGYGTLMAGVWRGSSLLSVWGADVYEFPYESRFKMWLIKRN---LLAATRIASTSHVMAEQTRSLCP 146
Cdd:cd03801    81 RKFDVVHAHglLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLARAealLRRADAVIAVSEALRDELRALGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 147 QLA-PIFITPFGIDTTRFVPVQKT----DDARLVIGTVKTMARKYGIDILIKGYALLRQRLQAEK-----ADDllgrlel 216
Cdd:cd03801   161 IPPeKIVVIPNGVDLERFSPPLRRklgiPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRlvivgGDG------- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 217 llvgggAETAALQALveQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRNdsESFGVAILEASSCALPVVVSRMGGLP 296
Cdd:cd03801   234 ------PLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRY--EGFGLVVLEAMAAGLPVVATDVGGLP 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532411019 297 EVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWEHCVTLMRDAY 358
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 20-355 5.73e-36

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: 134.68  E-value: 5.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  20 AMVEQGIEVHLITQHDFDALQYSDRVHVHMLPYRGGKG--YFLNRRALGKVLADLA-------------PDLLNCHYA-S 83
Cdd:cd03800    33 ALAELGYQVDIFTRRISPADPEVVEIAPGARVIRVPAGppEYLPKEELWPYLEEFAdgllrfiareggrYDLIHSHYWdS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  84 GY-GTLMAGVWR------GSSL-----LSVWGADVYEFPyeSRFKmwlIKRNLLAAT-RIASTSHVMAEQTRSLCPQLAP 150
Cdd:cd03800   113 GLvGALLARRLGvplvhtFHSLgrvkyRHLGAQDTYHPS--LRIT---AEEQILEAAdRVIASTPQEADELISLYGADPS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 151 -IFITPFGIDTTRFVPVQKTDDARLVIGT---------VKTMARKYGIDILIKGYA-LLRQRLQAEKA------DDLLGR 213
Cdd:cd03800   188 rINVVPPGVDLERFFPVDRAEARRARLLLppdkpvvlaLGRLDPRKGIDTLVRAFAqLPELRELANLVlvggpsDDPLSM 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 214 lelllvgggaETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMG 293
Cdd:cd03800   268 ----------DREELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSL--YEPFGLTAIEAMACGTPVVATAVG 335

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2532411019 294 GLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWE-HCVTLMR 355
Cdd:cd03800   336 GLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWEsVADQLLT 398
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 18-346 2.48e-35

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: 132.33  E-value: 2.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  18 CNAMVEQGIEVHLITqHDFDALQ---YSDRVHVHMLPY-RGGKGYFLNRRA---LGKVLADLAPDLLNCHYASG--YGTL 88
Cdd:cd03808    20 IKALVKKGYEVHVIA-PDGDKLSdelKELGVKVIDIPIlRRGINPLKDLKAlfkLYKLLKKEKPDIVHCHTPKPgiLGRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  89 MAGVWRGSSLLSV---WGadvYEFPYESRFKM---WLIKRNLLAATRIASTSHVMAEQTRSLC-PQLAPIFITP-FGIDT 160
Cdd:cd03808    99 AARLAGVPKVIYTvhgLG---FVFTEGKLLRLlylLLEKLALLFTDKVIFVNEDDRDLAIKKGiIKKKKTVLIPgSGVDL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 161 TRFVPVQK-TDDARLVIGTVKTMARKYGIDILIKGYALLRQRlqAEKAD-----DLLgrlelllvgggaETAALQALVEQ 234
Cdd:cd03808   176 DRFQYSPEsLPSEKVVFLFVARLLKDKGIDELIEAAKILKKK--GPNVRfllvgDGE------------LENPSEILIEK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 235 LGLGASVTFTGQVDHaaVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQ 314
Cdd:cd03808   242 LGLEGRIEFLGFRSD--VPELLAESDVFVLPSY--REGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVE 317

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2532411019 315 ALADALYQLVQDSALRTRLGVAGRARVCQQFS 346
Cdd:cd03808   318 ALADAIEKLIEDPELRKEMGEAARKRVEEKFD 349
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 155-345 5.39e-34

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: 128.72  E-value: 5.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 155 PFGIDTTRFVPVQKTDDARlVIGTVKTMARKYGIDILIKGYALLRQRlqaekaddlLGRLELLLVGGGAETAALQALVEQ 234
Cdd:cd05844   172 YIGIDPAKFAPRDPAERAP-TILFVGRLVEKKGCDVLIEAFRRLAAR---------HPTARLVIAGDGPLRPALQALAAA 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 235 LGlgaSVTFTGQVDHAAVPDWLNRLDIYVAASR----NDSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPN 310
Cdd:cd05844   242 LG---RVRFLGALPHAEVQDWMRRAEIFCLPSVtaasGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPE 318

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2532411019 311 ENPQALADALYQLVQDSALRTRLGVAGRARVCQQF 345
Cdd:cd05844   319 GDVDALADALQALLADRALADRMGGAARAFVCEQF 353
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 173-340 1.71e-32

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: 119.30  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 173 RLVIGTVKTMARKYGIDILIKGYALLRQRLQAEK---ADDLlgrlelllvgggAETAALQALVEQLGLGASVTFTGQVDH 249
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKlviAGDG------------EEEKRLKKLAEKLGLGDNVIFLGFVSD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 250 AAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSAL 329
Cdd:pfam00534  70 EDLPELLKIADVFVLPSR--YEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEEL 147

                         170
                  ....*....|.
gi 2532411019 330 RTRLGVAGRAR 340
Cdd:pfam00534 148 RERLGENARKR 158
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 42-358 8.30e-31

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: 120.11  E-value: 8.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  42 SDRVHVHMLPYRGGKGYFLNRRaLGKVLADLAPDLLNCHYASG--YGTLMAGVWRGSSLlsVWGA-DVYEFPYESRFKMW 118
Cdd:cd03807    49 AAGVPVVCLGLSSGKDPGVLLR-LAKLIRKRNPDVVHTWMYHAdlIGGLAAKLAGGVKV--IWSVrSSNIPQRLTRLVRK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 119 LikrNLLAATRIA---STSHVMAEQTRSLCPQLAPIFITPFGIDTTRFVPVQKT----------DDARLVIGTVKTMARK 185
Cdd:cd03807   126 L---CLLLSKFSPatvANSSAVAEFHQEQGYAKNKIVVIYNGIDLFKLSPDDASrararrrlglAEDRRVIGIVGRLHPV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 186 YGIDILIKGYALLRQRlqaekaddlLGRLELLLVGGGAETAALQALVEQLGLGASVTFTGQVDHaaVPDWLNRLDIYVAA 265
Cdd:cd03807   203 KDHSDLLRAAALLVET---------HPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLS 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 266 SRNdsESFGVAILEASSCALPVVVSRMGGLPEVVaENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQF 345
Cdd:cd03807   272 SRT--EGFPNALLEAMACGLPVVATDVGGAAELV-DDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEF 348

                         330
                  ....*....|...
gi 2532411019 346 SWEHCVTLMRDAY 358
Cdd:cd03807   349 SIDAMVRRYETLY 361
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
2-134 6.00e-29

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 108.95  E-value: 6.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   2 KIAILGPGNSIHISRWCNAMVEQGIEVHLITQHD-FDALQYSDRVHVHMLPY-RGGKGYFLNRRALGKVLADLAPDLLNC 79
Cdd:pfam13477   1 KILLLANADSIHTLRWADALADRGYDVHVISSKGpAKDELIAEGIHVHRLKVpRKGPLGYLKAFRLKKLIKKIKPDVVHV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2532411019  80 HYASGYGTLMAGVWRGSS----LLSVWGADVYEFPYESRFKMWLIKRNLLAATRIASTS 134
Cdd:pfam13477  81 HYAKPYGLLAGLAARLSGfppvVLSAWGLDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 255-363 3.17e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 106.61  E-value: 3.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 255 WLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLG 334
Cdd:COG0438    17 LLAAADVFVLPSR--SEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRRLG 94

                          90       100
                  ....*....|....*....|....*....
gi 2532411019 335 VAGRARVCQQFSWEHCVTLMRDAYVQTLA 363
Cdd:COG0438    95 EAARERAEERFSWEAIAERLLALYEELLA 123
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 2-350 9.54e-28

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: 112.05  E-value: 9.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   2 KIAILGP-------GNSIHISRWCNAMVEQGIEVHLITQH--------DFDALQYSDRVHVHMLPYRGGKGYFLNRRAL- 65
Cdd:cd03794     1 KILLISQyypppkgAAAARVYELAKELVRRGHEVTVLTPSpnyplgriFAGATETKDGIRVIRVKLGPIKKNGLIRRLLn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  66 ----------GKVLADLAPDLLncHYASGYGTLMAGVWRGSSLLSV-WGADVYEFPYESRFKMWLIKRNLL--------- 125
Cdd:cd03794    81 ylsfalaallKLLVREERPDVI--IAYSPPITLGLAALLLKKLRGApFILDVRDLWPESLIALGVLKKGSLlkllkkler 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 126 ----AATRIASTSHVMAEQTRSLCPQLAPIFITPFGIDTTRFVPVQKT-------DDARLVIGTVKTMARKYGIDILIKG 194
Cdd:cd03794   159 klyrLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDelrkklgLDDKFVVVYAGNIGKAQGLETLLEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 195 YALLRQRLQAEkaddllgrleLLLVGGGAETAALQALVEQLGLgASVTFTGQVDHAAVPDWLNRLDIYVAaSRNDSESFG 274
Cdd:cd03794   239 AERLKRRPDIR----------FLFVGDGDEKERLKELAKARGL-DNVTFLGRVPKEEVPELLSAADVGLV-PLKDNPANR 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 275 VAI----LEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWEHC 350
Cdd:cd03794   307 GSSpsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFSREKL 386
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 1-358 4.67e-27

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: 110.13  E-value: 4.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   1 MKIAIL-----GpGNSIHISRWCNAMVEQGIEVHLITQH-DFDALQYSDRVHVHMLpyrGGKGYFLNRR-----ALGKVL 69
Cdd:cd04962     1 MKIGIVcypsyG-GSGVVATELGLELAERGHEVHFISSAiPFRLNLYSGNIFFHEV---EVPNYPLFEYppytlALASKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  70 ADLAP----DLLNCHYA--SGYGTLMAGVWRGSSLLSV---WGADVYEFPYESRFKMwLIKRNLLAATRIASTSHVMAEQ 140
Cdd:cd04962    77 VEVAKehklDVLHAHYAipHASCAYLAREILGEKIPIVttlHGTDITLVGYDPSLQP-AVRFSINKSDRVTAVSSSLRQE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 141 TRSLCPQLAPIFITPFGIDTTRFVPVQKT---------DDARLVIgTVKTMARKYGIDILIKGYALLRQRLQAEkaddll 211
Cdd:cd04962   156 TYELFDVDKDIEVIHNFIDEDVFKRKPAGalkrrllapPDEKVVI-HVSNFRPVKRIDDVVRVFARVRRKIPAK------ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 212 grleLLLVGGGAETAALQALVEQLGLGASVTFTGQVDHaaVPDWLNRLDIYVAASrnDSESFGVAILEASSCALPVVVSR 291
Cdd:cd04962   229 ----LLLVGDGPERVPAEELARELGVEDRVLFLGKQDD--VEELLSIADLFLLPS--EKESFGLAALEAMACGVPVVSSN 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2532411019 292 MGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWEHCVTLMRDAY 358
Cdd:cd04962   301 AGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYY 367
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 14-347 2.33e-26

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: 107.83  E-value: 2.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  14 ISRWCNAMVEQGIEVHLITQHDFDALQYSDRVHVHMLPYRGGKGYFLNRR------ALGKVLADLAPDLL--NCHYASGY 85
Cdd:cd03811    18 LLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGllkailKLKRILKRAKPDVVisFLGFATYI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  86 GTLMAgvwRGSSLLSVWGADVYEFPYESRFKMWLIKRNLLAATRIASTSHVMAEQTRSLCPQLA-PIFITPFGIDTTRFV 164
Cdd:cd03811    98 VAKLA---AARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPeKIEVIYNPIDIDRIR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 165 -----PVQKTDDARLVIGTVKTMARKYGIDILIKGYALLRQRLQAEKA------DDLlgrlelllvgggaetAALQALVE 233
Cdd:cd03811   175 alakePILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLvilgdgPLR---------------EELEKLAK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 234 QLGLGASVTFTGQVDhaAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENP 313
Cdd:cd03811   240 ELGLAERVIFLGFQS--NPYPYLKKADLFVLSSR--YEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDA 315

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2532411019 314 QALA---DALYQLVQDSALRTRLGvAGRARVCQQFSW 347
Cdd:cd03811   316 AALAgilAALLQKKLDAALRERLA-KAQEAVFREYTI 351
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
224-326 8.06e-26

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 100.66  E-value: 8.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 224 ETAALQALVEqlGLGASVTFTGQVDhaAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVaENE 303
Cdd:pfam13692  43 PEEELEELAA--GLEDRVIFTGFVE--DLAELLAAADVFVLPSL--YEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGE 115

                          90       100
                  ....*....|....*....|...
gi 2532411019 304 TGLIIPNENPQALADALYQLVQD 326
Cdd:pfam13692 116 NGLLVPPGDPEALAEAILRLLED 138
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 14-358 2.18e-25

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: 105.07  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  14 ISRWCNAMVEQGIEVHLITQHDFDALQYS--DRVHVHMLPYRGGKGYFL---NRRALGKVLADLAPDLLnchYASGYGTL 88
Cdd:cd03814    20 LERLVDHLRRRGHEVRVVAPGPFDEAESAegRVVSVPSFPLPFYPEYRLalpLPRRVRRLIKEFQPDII---HIATPGPL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  89 magVWRGSSLLSVWGADV---Y--EFP-YESRFKMWLIKRNLLA--------ATRIASTSHVMAEQ-TRSLCPQLAPIfi 153
Cdd:cd03814    97 ---GLAALRAARRLGLPVvtsYhtDFPeYLSYYTLGPLSWLAWAylrwfhnpFDTTLVPSPSIARElEGHGFERVRLW-- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 154 tPFGIDTTRFVPVQKT--------DDARLVIGTVKTMARKYGIDILIKGYALLRQRLQAEKA---DDllgrlelllvggg 222
Cdd:cd03814   172 -PRGVDTELFHPSRRDaalrrrlgPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVvvgDG------------- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 223 AETAALQALveqlglGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAEN 302
Cdd:cd03814   238 PARAELEAR------GPDVIFTGFLTGEELARAYASADVFVFPSR--TETFGLVVLEAMASGLPVVAADAGGPRDIVRPG 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2532411019 303 ETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVcQQFSWEHCVTLMRDAY 358
Cdd:cd03814   310 GTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEA-ERYSWEAFLDNLLDYY 364
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 20-346 3.89e-24

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: 101.64  E-value: 3.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  20 AMVEQGIEVHLITQH-----DFDALQYSDRVHVHMLpyrggKGYFLNRRALGKVLADLA-------PDLLN--CHYASGy 85
Cdd:cd03825    25 ALLAYGIDSTMLVGRkknliSKPEFIEADIIHLHWI-----HGGYLSLKALFKLLRRKPvvwtlhdMWPFTggCHYPME- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  86 gtlmAGVWRGSSLLSVWGADVYEFPYESRFKMWLIKRNLLAATR--IASTSHVMAEQTRS---LCPQlaPIFITPFGIDT 160
Cdd:cd03825    99 ----CEGWKTGCGNCPNLNSYPPAKKDLSRQLFRRKREALAKKRltIVAPSRWLADMVRRsplLKGL--PVVVIPNGIDT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 161 TRFVPVQKtDDARLVIGTVKT----MARKYGIDILIKGYALLrqrlqaekaddllgrlelllvgggaeTAALQALVEQ-- 234
Cdd:cd03825   173 EIFAPVDK-AKARKRLGIPQDkkviLFGAESVTKPRKGFDEL--------------------------IEALKLLATKdd 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 235 -----LGLGASVTFTGQVDHAAVP---------DWLNRLDIYVAASRNDSesFGVAILEASSCALPVVVSRMGGLPEVVA 300
Cdd:cd03825   226 lllvvFGKNDPQIVILPFDIISLGyidddeqlvDIYSAADLFVHPSLADN--LPNTLLEAMACGTPVVAFDTGGSPEIVQ 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2532411019 301 ENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFS 346
Cdd:cd03825   304 HGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFD 349
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 2-349 4.48e-24

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: 101.16  E-value: 4.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   2 KIAILGPgnSIH--------ISRWCNAMVEQGIEVHLITQHDFDALQY---SDRVHVHML------PYRGGKGYFLNRRA 64
Cdd:cd03820     1 KIAIVIP--SISnaggaervAINLANHLAKKGYDVTIISLDSAEKPPFyelDDNIKIKNLgdrkysHFKLLLKYFKKVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  65 LGKVLADLAPDLLnchyasgYGTLMagvwRGSSLLSVWGADV---------YEFPYESRFKMWLIKRNLLAATRIAstsh 135
Cdd:cd03820    79 LRKYLKNNKPDVV-------ISFRT----SLLTFLALIGLKSklivwehnnYEAYNKGLRRLLLRRLLYKRADKIV---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 136 VMAEQTRSLCPQ--LAPIFITPFGIDttrFVPVQKTDD--ARLVIgTVKTMARKYGIDILIKGYALLRQRLQAEKAD--- 208
Cdd:cd03820   144 VLTEADKLKKYKqpNSNVVVIPNPLS---FPSEEPSTNlkSKRIL-AVGRLTYQKGFDLLIEAWALIAKKHPDWKLRiyg 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 209 DLLgrlelllvgggaETAALQALVEQLGLGASVTFTGQVDHAAvpDWLNRLDIYVAASRNdsESFGVAILEASSCALPVV 288
Cdd:cd03820   220 DGP------------EREELEKLIDKLGLEDRVKLLGPTKNIA--EEYANSSIFVLSSRY--EGFPMVLLEAMAYGLPII 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532411019 289 VS-RMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVcQQFSWEH 349
Cdd:cd03820   284 SFdCPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEK 344
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 118-350 1.46e-23

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: 100.13  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 118 WLIKRNLLAATRIASTSHVMAEQTRSLCP-QLAPIFITPFGIDTTRFVPVQKTDDAR---------LVIGTVKtmARKyG 187
Cdd:cd03809   130 LLLPISLRRADAIITVSEATRDDIIKFYGvPPEKIVVIPLGVDPSFFPPESAAVLIAkyllpepyfLYVGTLE--PRK-N 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 188 IDILIKGYALLRQRLQ------AEKADDllgrlelllvgggaETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDI 261
Cdd:cd03809   207 HERLLKAFALLKKQGGdlklviVGGKGW--------------EDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARA 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 262 YVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENetGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARV 341
Cdd:cd03809   273 FVFPSL--YEGFGLPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDPLDPESIADAILRLLEDPSLREELIRKGLERA 348


                  ....*....
gi 2532411019 342 cQQFSWEHC 350
Cdd:cd03809   349 -KKFSWEKT 356
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 9-343 1.56e-23

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: 100.05  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019   9 GNSIHISRWCNAMVEQGIEVHLITQHDFDAlQYSDRVHVHMLPYRGGKGY------FLNRRALGKVLADLAPDLlnCHYA 82
Cdd:cd03817    15 GVATSVRNLARALEKRGHEVYVITPSDPGA-EDEEEVVRYRSFSIPIRKYhrqhipFPFKKAVIDRIKELGPDI--IHTH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  83 SGYGTLMAG--VWRGSSLLSV------WGADVYEFPyesrfKMWLIKRNLLAATRIA---STSHVmaeqtrsLCPQLA-- 149
Cdd:cd03817    92 TPFSLGKLGlrIARKLKIPIVhtyhtmYEDYLHYIP-----KGKLLVKAVVRKLVRRfynHTDAV-------IAPSEKik 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 150 ----------PIFITPFGIDTTRFVPVQKTDDARL--------VIGTVKTMARKYGIDILIKGYALLRQRLQAE---KAD 208
Cdd:cd03817   160 dtlreygvkgPIEVIPNGIDLDKFEKPLNTEERRKlglppdepILLYVGRLAKEKNIDFLLRAFAELKKEPNIKlviVGD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 209 dllgrlelllvggGAETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASrnDSESFGVAILEASSCALPVV 288
Cdd:cd03817   240 -------------GPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFAS--TTETQGLVYLEAMAAGLPVV 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2532411019 289 VSRMGGLPEVVAENETGLIIPnENPQALADALYQLVQDSALRTRLGVAGRARVCQ 343
Cdd:cd03817   305 AAKDPAASELVEDGENGFLFE-PNDETLAEKLLHLRENLELLRKLSKNAEISARE 358
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 116-348 2.63e-23

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: 99.37  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 116 KMWLIKRNLLAATRIASTSHVMAEQTRSLCPQlAPIFITPFGIDTTRFVP-------VQKTDDARLVIGTVKTMARKyGI 188
Cdd:cd03821   142 LHLIERRNLNNAALVHFTSEQEADELRRFGLE-PPIAVIPNGVDIPEFDPglrdrrkHNGLEDRRIILFLGRIHPKK-GL 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 189 DILIKGYAllrqRLQAEKADdllGRLELLLVGGGAETAALQALVEqLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRn 268
Cdd:cd03821   220 DLLIRAAR----KLAEQGRD---WHLVIAGPDDGAYPAFLQLQSS-LGLGDRVTFTGPLYGEAKWALYASADLFVLPSY- 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 269 dSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPneNPQALADALYQLVQDSALRTRLGVAGRA--RVCQQFS 346
Cdd:cd03821   291 -SENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDP--NVSSLAEALAEALRDPADRKRLGEMARRarQVEENFS 367


                  ..
gi 2532411019 347 WE 348
Cdd:cd03821   368 WE 369
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 115-346 2.06e-21

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: 93.88  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 115 FKMWLIKRnllaATRIASTSHVMAEQTRSLCPQLAPIFITPFGIDTTRFVPVQKTDDAR----------LVIGTVktmaR 184
Cdd:cd03795   130 LMTRFLRR----ADRIIATSPNYVETSPTLREFKNKVRVIPLGIDKNVYNIPRVDFENIkrekkgkkifLFIGRL----V 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 185 KY-GIDILIKgyallrqrlqAEKADDLLGRLELLLVgggaETAALQALVEqLGLGASVTFTGQVDHAAVPDWLNRLDIYV 263
Cdd:cd03795   202 YYkGLDYLIE----------AAQYLNYPIVIGGEGP----LKPDLEAQIE-LNLLDNVKFLGRVDDEEKVIYLHLCDVFV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 264 AASRNDSESFGVAILEASSCALPVVVSRMG-GLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVC 342
Cdd:cd03795   267 FPSVLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRFE 346


                  ....
gi 2532411019 343 QQFS 346
Cdd:cd03795   347 ELFT 350
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 151-358 2.36e-20

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 92.01  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 151 IFITPFGIDTTRFVPVQKTDDAR--LVIGTVKTMARKYGIDILIKGYALLRQRLqaEKADDLLGRLELLLVGGGAETaal 228
Cdd:cd03813   269 TRVIPNGIDIQRFAPAREERPEKepPVVGLVGRVVPIKDVKTFIRAFKLVRRAM--PDAEGWLIGPEDEDPEYAQEC--- 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 229 QALVEQLGLGASVTFTGQVDhaaVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVV-----AENE 303
Cdd:cd03813   344 KRLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSI--SEGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQ 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2532411019 304 TGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWEHCVTLMRDAY 358
Cdd:cd03813   419 AGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 20-338 5.98e-18

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: 83.94  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  20 AMVEQGIEVH------LITQHDFDALQYSDR-----------VHVHMLPYRGGKgYFLNRRALGKVLADLAPDLLNCHyA 82
Cdd:cd03819     7 ALEIGGAETYildlarALAERGHRVLVVTAGgpllprlrqigIGLPGLKVPLLR-ALLGNVRLARLIRRERIDLIHAH-S 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  83 SGYGTLMAGVWRGSSL---LSVWGadVYEFPYESRFKMWLIKRNllaATRIASTSHVMAEQT-RSLCPQLAPIFITPFGI 158
Cdd:cd03819    85 RAPAWLGWLASRLTGVplvTTVHG--SYLATYHPKDFALAVRAR---GDRVIAVSELVRDHLiEALGVDPERIRVIPNGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 159 DTTRFVPVQK--------TDDARLVIGTVKTMARKYGIDILIKGYALLRQRLQAEK--ADDLlgrlelllvgggAETAAL 228
Cdd:cd03819   160 DTDRFPPEAEaeeraqlgLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLlvAGDG------------PERDEI 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 229 QALVEQLGLGASVTFTGQVDhaAVPDWLNRLDIYVAASRNdsESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLII 308
Cdd:cd03819   228 RRLVERLGLRDRVTFTGFRE--DVPAALAASDVVVLPSLH--EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLV 303

                         330       340       350
                  ....*....|....*....|....*....|
gi 2532411019 309 PNENPQALADALYQLVQDSALRTRLGVAGR 338
Cdd:cd03819   304 PPGDAEALADAIRAAKLLPEAREKLQAAAA 333
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 151-345 6.49e-16

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: 77.88  E-value: 6.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 151 IFITPFGIDTTRFVPVQKTD--DARLVIGTVKTMARKYGIDILIKGYALLRQR---LQAEKADDLLGRlelllvgggaet 225
Cdd:cd03799   150 IIVHRSGIDCNKFRFKPRYLplDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKypnIEYQIIGDGDLK------------ 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 226 AALQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAAS----RNDSESFGVAILEASSCALPVVVSRMGGLPEVVAE 301
Cdd:cd03799   218 EQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSvtaaDGDQDGPPNTLKEAMAMGLPVISTEHGGIPELVED 297

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2532411019 302 NETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQF 345
Cdd:cd03799   298 GVSGFLVPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 62-341 1.28e-15

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: 76.98  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  62 RRALGKVLADLAPDLLNCHYASGYGtlmAGVWR--------------------GSSLLSVWGADVYEFPyeSRFKMWLIK 121
Cdd:cd03823    85 RRLLARLLEDFRPDVVHTHNLSGLG---ASLLDaardlgipvvhtlhdywllcPRQFLFKKGGDAVLAP--SRFTANLHE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 122 RNLLAATRIastsHVMaeqtrslcpqlapifitPFGIDTTRFVPVQKTD-DARLVIGTVKTMARKYGIDILIKGYALLRQ 200
Cdd:cd03823   160 ANGLFSARI----SVI-----------------PNAVEPDLAPPPRRRPgTERLRFGYIGRLTEEKGIDLLVEAFKRLPR 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 201 ---RLQ-AEKADDLLGrlelllvgggaetaalqalvEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRNDsESFGVA 276
Cdd:cd03823   219 ediELViAGHGPLSDE--------------------RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWP-EPFGLV 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532411019 277 ILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARV 341
Cdd:cd03823   278 VREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPR 342
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 117-356 1.34e-12

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 68.58  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 117 MWLIKRNLLAATRIA-STSHVMAEQTRSLCPQLAP-IFITPFGIDTTRFVPVQKTDDARL----------VIGTV----- 179
Cdd:PLN02871  195 MWDIIRFLHRAADLTlVTSPALGKELEAAGVTAANrIRVWNKGVDSESFHPRFRSEEMRArlsggepekpLIVYVgrlga 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 180 --------KTMARKYGIDILIKGYALLRQRLqaekaddllgrlelllvgggaetaalqalvEQLGLGASVTFTGQVDHAA 251
Cdd:PLN02871  275 eknldflkRVMERLPGARLAFVGDGPYREEL------------------------------EKMFAGTPTVFTGMLQGDE 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 252 VPDWLNRLDIYVAASrnDSESFGVAILEASSCALPVVVSRMGGLPEVVA---ENETGLIIPnenPQALADA---LYQLVQ 325
Cdd:PLN02871  325 LSQAYASGDVFVMPS--ESETLGFVVLEAMASGVPVVAARAGGIPDIIPpdqEGKTGFLYT---PGDVDDCvekLETLLA 399

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2532411019 326 DSALRTRLGVAGRARVcQQFSWEHCVTLMRD 356
Cdd:PLN02871  400 DPELRERMGAAAREEV-EKWDWRAATRKLRN 429
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 150-351 2.41e-12

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: 66.94  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 150 PIFITPFGIDTTRFVPVQKTDDARLVIGTVKTMARKYGIDILIKGYALLRQRLQAEKADdllgrlellLVGGGAETAALQ 229
Cdd:cd04949   137 PIFTIPVGYVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLD---------IYGYGEEREKLK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 230 ALVEQLGLGASVTFTGQvdHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMG-GLPEVVAENETGLII 308
Cdd:cd04949   208 KLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTSQ--MEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLI 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2532411019 309 PNENPQALADALYQLVQDSALRTRLGVAGRArVCQQFSWEHCV 351
Cdd:cd04949   284 EKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYSTENVM 325
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 187-308 4.59e-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: 65.12  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 187 GIDILIKGYALLRQRLQAekaddllgrLELLLVGGGAETAALQALVEQLGLGASVTFTGQVDHAAVPDWLNRL-DIYVAA 265
Cdd:cd01635   124 GIDLLLEALALLKARLPD---------LVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLP 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2532411019 266 SRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLII 308
Cdd:cd01635   195 SR--SEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 228-327 1.96e-11

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: 64.39  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 228 LQALVEQLGLGASVTFTGQVDHaaVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENEtgLI 307
Cdd:cd04951   234 LERLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSE--WEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN--YV 307

                          90       100
                  ....*....|....*....|
gi 2532411019 308 IPNENPQALADALYQLVQDS 327
Cdd:cd04951   308 VPVSDPQLLAEKIKEIFDMS 327
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 228-320 1.96e-10

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 61.49  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 228 LQALVEQLGLGASVTFTGQVDHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLI 307
Cdd:cd03796   239 LEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSL--TEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLA 316

                          90
                  ....*....|...
gi 2532411019 308 IPneNPQALADAL 320
Cdd:cd03796   317 EP--DPEDIVRKL 327
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 228-313 6.47e-10

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 60.17  E-value: 6.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 228 LQALVEQLGLGASVTFTGQVDHAAVPDWL--NRLDIYVAASrnDSESFGVAILEASSCALPVVVSRMGGLPEVVaENETG 305
Cdd:cd04946   272 LEKLAENKLENVKVNFTGEVSNKEVKQLYkeNDVDVFVNVS--ESEGIPVSIMEAISFGIPVIATNVGGTREIV-ENETN 348


                  ....*...
gi 2532411019 306 LIIPNENP 313
Cdd:cd04946   349 GLLLDKDP 356
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 231-352 1.63e-09

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


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 59.41  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  231 LVEQLGLGASVTFTGQVDHAAVPDwlnrldIYVAASRNDS--------ESFGVAILEASSCALPVVVSRMGGLPEVVAEN 302
Cdd:TIGR02468  540 LIDKYDLYGQVAYPKHHKQSDVPD------IYRLAAKTKGvfinpafiEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVL 613

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2532411019  303 ETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVcQQFSW-EHCVT 352
Cdd:TIGR02468  614 DNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNI-HLFSWpEHCKT 663
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 229-351 1.82e-09

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 58.53  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 229 QALVEQLGLGAS-VTFTGQVDHAAVPDWLNRLDIYVAASRNDSESFGVaiLEASSCALPVVVSRMGGLPEVVAENETGLI 307
Cdd:cd03818   270 QKMLAELGVDLErVHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIRDGRNGLL 347

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2532411019 308 IPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSWEHCV 351
Cdd:cd03818   348 VDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 271-346 5.80e-09

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 57.21  E-value: 5.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2532411019 271 ESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNeNPQALADALYQLVQDSALRTRLGVAGRARVCQQFS 346
Cdd:cd03805   310 EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFS 384
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
261-356 7.55e-09

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 52.61  E-value: 7.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 261 IYVAASRNDsESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIpnENPQALADALYQLVQDSALRTRLGVAGRAR 340
Cdd:pfam13524   1 IVLNPSRRP-DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRER 77

                          90
                  ....*....|....*.
gi 2532411019 341 VCQQFSWEHCVTLMRD 356
Cdd:pfam13524  78 VLAEHTYAHRAEQLLD 93
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 271-345 1.44e-08

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 55.79  E-value: 1.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532411019 271 ESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPneNPQALADALYQLVQDSALRTRLGVAGRARVCQQF 345
Cdd:cd03792   290 EGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVN--SVEGAAVRILRLLTDPELRRKMGLAAREHVRDNF 362
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 233-363 3.01e-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: 54.60  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 233 EQLGLGASVTFTGQVDHaavpDWLNRLdiyVAASR------NDSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGL 306
Cdd:cd03802   214 QEPLPGPRIEFIGEVGH----DEKQEL---LGGARallfpiNWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGF 286

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2532411019 307 IIPneNPQALADALYQLvqdSALRTRlgvAGRARVCQQFSWEHCVtlmrDAYVQTLA 363
Cdd:cd03802   287 LVD--SVEEMAEAIANI---DRIDRA---ACRRYAEDRFSAARMA----DRYEALYR 331
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
13-160 5.04e-08

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 52.15  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  13 HISRWCNAMVEQGIEVHLITQHDFDALQYSDR--VHVHMLPYRGGKGY---FLNRRALGKVLADLAPDLLNCHYASGYGT 87
Cdd:pfam13439   6 YVLELARALARRGHEVTVVTPGGPGPLAEEVVrvVRVPRVPLPLPPRLlrsLAFLRRLRRLLRRERPDVVHAHSPFPLGL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  88 LMAGVWRGS---------SLLSVWGADVYEFPYESRFKMWLIKRNLLAATRIASTSHVMAEQTRSLCP-QLAPIFITPFG 157
Cdd:pfam13439  86 AALAARLRLgiplvvtyhGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGvPPEKIRVIPNG 165


                  ...
gi 2532411019 158 IDT 160
Cdd:pfam13439 166 VDL 168
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
114-340 2.65e-07

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 51.90  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 114 RFKMWLIKRNLLAATRIASTSHVMAEQTRSLCPQLAPIFITPFGIDTTRFVPVQKTDD----ARLVIGTVKT-------M 182
Cdd:PRK10307  159 RLATAFERSLLRRFDNVSTISRSMMNKAREKGVAAEKVIFFPNWSEVARFQPVADADVdalrAQLGLPDGKKivlysgnI 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 183 ARKYGIDILIKGYALLRQRlqaekaddllGRLELLLVGGGAETAALQALVEQLGLgASVTFTGQVDHAAVPDWLNRLDIY 262
Cdd:PRK10307  239 GEKQGLELVIDAARRLRDR----------PDLIFVICGQGGGKARLEKMAQCRGL-PNVHFLPLQPYDRLPALLKMADCH 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 263 VAASRNDsesfgvaileASSCALP-------------VVVSRMG-GLPEVVAENetGLIIPNENPQALADALYQLVQDSA 328
Cdd:PRK10307  308 LLPQKAG----------AADLVLPskltnmlasgrnvVATAEPGtELGQLVEGI--GVCVEPESVEALVAAIAALARQAL 375

                         250
                  ....*....|..
gi 2532411019 329 LRTRLGVAGRAR 340
Cdd:PRK10307  376 LRPKLGTVAREY 387
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
13-157 2.91e-07

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 49.71  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019  13 HISRWCNAMVEQGIEVHLITQHDFDALQYSDR-----VHVHMLPYRGGKGYFLNRRALGKVLADLAPDLLNCHYA-SGYG 86
Cdd:pfam13579   6 YVLELARALAALGHEVRVVTPGGPPGRPELVGdgvrvHRLPVPPRPSPLADLAALRRLRRLLRAERPDVVHAHSPtAGLA 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2532411019  87 TLMAGVWRGSSL-LSVWGAD-VYEFPYESRFKMWLIKRNLLAATRIASTSHVMAEQTRSLCPQLAPIFITPFG 157
Cdd:pfam13579  86 ARLARRRRGVPLvVTVHGLAlDYGSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAARVVVVPNG 158
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 228-346 1.38e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 50.03  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 228 LQALVEQLGLGASVTFTGQVDHaaVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLI 307
Cdd:PRK15179  563 VREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSR--FEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLT 638

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2532411019 308 IPNENPQA--LADALYQLVQDSALRTRLGVAGRARVCQQFS 346
Cdd:PRK15179  639 LPADTVTApdVAEALARIHDMCAADPGIARKAADWASARFS 679
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 120-349 7.43e-06

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: 47.38  E-value: 7.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 120 IKRNLLAATRIAstshVMAEQTRSLC-----PQLAPIFITPFGIDTTRFVPVQKTD-----DARLVIGTVKTMARKYGID 189
Cdd:cd03822   128 LFRIATLSERVV----VMAPISRFLLvriklIPAVNIEVIPHGVPEVPQDPTTALKrlllpEGKKVILTFGFIGPGKGLE 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 190 ILIKGYALLRQRLQ-------AEKADDLLGRLELllvgggaetAALQALVEQLGLGASVTF-TGQVDHAAVPDWLNRLDI 261
Cdd:cd03822   204 ILLEALPELKAEFPdvrlviaGELHPSLARYEGE---------RYRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADV 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 262 YVAASRNDSESFGVAILEASSCALPVVVSRMGGLPEVVAENEtGLIIPNENPQALADALYQLVQDS----ALRTRLGVAG 337
Cdd:cd03822   275 VVLPYLNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAILRLLEDDerrqAIAERAYAYA 353

                         250
                  ....*....|..
gi 2532411019 338 RArvcqqFSWEH 349
Cdd:cd03822   354 RA-----MTWES 360
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 238-325 7.78e-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: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 238 GASVTFTGQVDHAAVPDWLNRLDIYVAASRNDsesFGVAILEASSCALPVVVSRMGGLPEVVAENETGLIIPNENPQALA 317
Cdd:cd03804   245 SPNVEFLGYQPDEVLKELLSKARAFVFAAEED---FGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLK 321


                  ....*...
gi 2532411019 318 DALYQLVQ 325
Cdd:cd03804   322 AAVEEFEQ 329
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 230-358 3.96e-05

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 45.31  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 230 ALVEQLGLGASVTFTG--QVDhaavpDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMG-------GL-PEVV 299
Cdd:NF038011  358 SLVASLGLQDKVKFLGfqKID-----DLLPQVGLMVLSSI--SEALPLVVLEAFAAGVPVVTTDVGscrqlieGLdEEDR 430

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2532411019 300 AENETGLIIPNENPQALADALYQLVQDSALRTRLGVAGRARVCQQFSwehcVTLMRDAY 358
Cdd:NF038011  431 ALGAAGEVVAIADPQALARAALDLLRDPQRWQAAQAAGLARVERYYT----EELMFDRY 485
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 228-314 3.96e-05

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


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 44.97  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 228 LQALVEQLGLGASVTFTGQVDHaaVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETGLI 307
Cdd:cd03812   237 IKEKVKELGLEDKVIFLGFRND--VSEILSAMDVFLFPSL--YEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLP 312


                  ....*..
gi 2532411019 308 IpNENPQ 314
Cdd:cd03812   313 L-NETPS 318
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
226-363 8.22e-04

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 41.22  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 226 AALQALVEQLGLGASVTFTGQvdHAAVPDWLNRLDIYVAASRndSESFGVAILEASSCALPVVVSRMGGLPEVVAENETG 305
Cdd:PRK15490  442 AEAQKRAEQLGILERILFVGA--SRDVGYWLQKMNVFILFSR--YEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSG 517

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2532411019 306 LIIPNENPQALADAL-YQLVQDSALRTRLGVAGRAR--VCQQFSWEHcvtlMRDAYVQTLA 363
Cdd:PRK15490  518 FILDDAQTVNLDQACrYAEKLVNLWRSRTGICQQTQsfLQERFTVEH----MVGTFVKTIA 574
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
271-349 1.13e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 40.54  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532411019 271 ESFGVAILEASSCALPVVVSRMGGLPEVVAENETG--LIIPnENPQALADALYQLVQDSAlRTRLGVAGRARVCQQFSWE 348
Cdd:PRK15484  288 EAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGyhLAEP-MTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWE 365


                  .
gi 2532411019 349 H 349
Cdd:PRK15484  366 G 366
 
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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