NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1015427105|gb|AMV08896|]
View 

GDP-mannose:glycolipid 4-beta-D-mannosyltransferase [Xanthomonas citri pv. aurantifolii]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
59-337 6.14e-17

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 cd03822:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 370  Bit Score: 80.89  E-value: 6.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  59 SRYDVLHLHWPEYLLRHPTTAGTLAKQvcaallllklQLTGTPVVRTLHNLA-----PHEDRGWRERSLLRWIDRLTRRW 133
Cdd:cd03822    74 KKPDVVHIQHEFGIFGGKYGLYALGLL----------LHLRIPVITTLHTVLdlsdpGKQALKVLFRIATLSERVVVMAP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 134 IRIN-ATTPPRPPFTDTIL--HGHYRDWFASMEQ-----GSTVPGRLLHFGLIRPYKGVETLLEVMRGVNDA--RLSLRI 203
Cdd:cd03822   144 ISRFlLVRIKLIPAVNIEVipHGVPEVPQDPTTAlkrllLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVI 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 204 VGNPATPQMRNLVEHACAQ-------DPRISALLAYVEEPVLAREVSAAELVVLPYRQMH--NSGTLLLALSLARPVLAP 274
Cdd:cd03822   224 AGELHPSLARYEGERYRKAaieelglQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEqsSSGTLSYAIACGKPVIST 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 275 --WSESNAAIAEEvgpGWVFLYEDEFD-AALLTGVLD----KVRAAPRGPAPdLSQRDWPRIGQLHYRTY 337
Cdd:cd03822   304 plRHAEELLADGR---GVLVPFDDPSAiAEAILRLLEdderRQAIAERAYAY-ARAMTWESIADRYLRLF 369
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
59-337 6.14e-17

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: 80.89  E-value: 6.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  59 SRYDVLHLHWPEYLLRHPTTAGTLAKQvcaallllklQLTGTPVVRTLHNLA-----PHEDRGWRERSLLRWIDRLTRRW 133
Cdd:cd03822    74 KKPDVVHIQHEFGIFGGKYGLYALGLL----------LHLRIPVITTLHTVLdlsdpGKQALKVLFRIATLSERVVVMAP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 134 IRIN-ATTPPRPPFTDTIL--HGHYRDWFASMEQ-----GSTVPGRLLHFGLIRPYKGVETLLEVMRGVNDA--RLSLRI 203
Cdd:cd03822   144 ISRFlLVRIKLIPAVNIEVipHGVPEVPQDPTTAlkrllLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVI 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 204 VGNPATPQMRNLVEHACAQ-------DPRISALLAYVEEPVLAREVSAAELVVLPYRQMH--NSGTLLLALSLARPVLAP 274
Cdd:cd03822   224 AGELHPSLARYEGERYRKAaieelglQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEqsSSGTLSYAIACGKPVIST 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 275 --WSESNAAIAEEvgpGWVFLYEDEFD-AALLTGVLD----KVRAAPRGPAPdLSQRDWPRIGQLHYRTY 337
Cdd:cd03822   304 plRHAEELLADGR---GVLVPFDDPSAiAEAILRLLEdderRQAIAERAYAY-ARAMTWESIADRYLRLF 369
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
171-273 2.34e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 43.65  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 171 RLLHFG-LIRPYKGVETLLEVMRGV--NDARLSLRIVGNPAtpqMRNLVEHACAQDPRISaLLAYVEEpvLAREVSAAEL 247
Cdd:pfam13692   3 VILFVGrLHPNVKGVDYLLEAVPLLrkRDNDVRLVIVGDGP---EEELEELAAGLEDRVI-FTGFVED--LAELLAAADV 76
                          90       100
                  ....*....|....*....|....*.
gi 1015427105 248 VVLPYRQMHNSGTLLLALSLARPVLA 273
Cdd:pfam13692  77 FVLPSLYEGFGLKLLEAMAAGLPVVA 102
 
Name Accession Description Interval E-value
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
59-337 6.14e-17

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: 80.89  E-value: 6.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  59 SRYDVLHLHWPEYLLRHPTTAGTLAKQvcaallllklQLTGTPVVRTLHNLA-----PHEDRGWRERSLLRWIDRLTRRW 133
Cdd:cd03822    74 KKPDVVHIQHEFGIFGGKYGLYALGLL----------LHLRIPVITTLHTVLdlsdpGKQALKVLFRIATLSERVVVMAP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 134 IRIN-ATTPPRPPFTDTIL--HGHYRDWFASMEQ-----GSTVPGRLLHFGLIRPYKGVETLLEVMRGVNDA--RLSLRI 203
Cdd:cd03822   144 ISRFlLVRIKLIPAVNIEVipHGVPEVPQDPTTAlkrllLPEGKKVILTFGFIGPGKGLEILLEALPELKAEfpDVRLVI 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 204 VGNPATPQMRNLVEHACAQ-------DPRISALLAYVEEPVLAREVSAAELVVLPYRQMH--NSGTLLLALSLARPVLAP 274
Cdd:cd03822   224 AGELHPSLARYEGERYRKAaieelglQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEqsSSGTLSYAIACGKPVIST 303
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 275 --WSESNAAIAEEvgpGWVFLYEDEFD-AALLTGVLD----KVRAAPRGPAPdLSQRDWPRIGQLHYRTY 337
Cdd:cd03822   304 plRHAEELLADGR---GVLVPFDDPSAiAEAILRLLEdderRQAIAERAYAY-ARAMTWESIADRYLRLF 369
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
54-310 1.83e-10

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: 61.40  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  54 RDALLSRYDVLHLHWPeyllrhpttagtlakqVCAALLLLKLQLTGTPVVRTLHNLAPHEDRGWRERSLlRWIDRLTRRW 133
Cdd:cd03801    76 PLLRLRKFDVVHAHGL----------------LAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAER-RLLARAEALL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 134 IRINATT--------------PPRPPFTDTILHG----HYRDWFASMEQGSTVPGRLLHFGLIRPYKGVETLLEVMRGVN 195
Cdd:cd03801   139 RRADAVIavsealrdelralgGIPPEKIVVIPNGvdleRFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 196 DAR--LSLRIVGnPATPQMRNLVEHACAQDPRISaLLAYVEEPVLAREVSAAELVVLPYRQMHNSGTLLLALSLARPVLA 273
Cdd:cd03801   219 RRGpdVRLVIVG-GDGPLRAELEELELGLGDRVR-FLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVA 296
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1015427105 274 pwseSNA-AIAEEVGPGWVFLYEDEFDAALLTGVLDKV 310
Cdd:cd03801   297 ----TDVgGLPEVVEDGEGGLVVPPDDVEALADALLRL 330
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
171-273 2.34e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 43.65  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 171 RLLHFG-LIRPYKGVETLLEVMRGV--NDARLSLRIVGNPAtpqMRNLVEHACAQDPRISaLLAYVEEpvLAREVSAAEL 247
Cdd:pfam13692   3 VILFVGrLHPNVKGVDYLLEAVPLLrkRDNDVRLVIVGDGP---EEELEELAAGLEDRVI-FTGFVED--LAELLAAADV 76
                          90       100
                  ....*....|....*....|....*.
gi 1015427105 248 VVLPYRQMHNSGTLLLALSLARPVLA 273
Cdd:pfam13692  77 FVLPSLYEGFGLKLLEAMAAGLPVVA 102
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
62-309 1.14e-03

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: 40.39  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  62 DVLHLHwpeYLLRHPTTAGTLAKQvcaallllklqlTGTPVVRTLHNLAPHEDRGWRER-------SLLRWIDRLTRRW- 133
Cdd:cd03823    98 DVVHTH---NLSGLGASLLDAARD------------LGIPVVHTLHDYWLLCPRQFLFKkggdavlAPSRFTANLHEANg 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 134 ---IRI----NATTPPRPPFTdtilhghyRDWFasmeqgSTVPGRLLHFGLIRPYKGVETLLEVMRGVNDARLSLRIVGN 206
Cdd:cd03823   163 lfsARIsvipNAVEPDLAPPP--------RRRP------GTERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGH 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 207 PatpqmRNLVEHACAQDPRISALLAYVEEPvLAREVSAAELVVLPYRQMHNSG-TLLLALSLARPVLApwsESNAAIAEE 285
Cdd:cd03823   229 G-----PLSDERQIEGGRRIAFLGRVPTDD-IKDFYEKIDVLVVPSIWPEPFGlVVREAIAAGLPVIA---SDLGGIAEL 299
                         250       260
                  ....*....|....*....|....*...
gi 1015427105 286 VGP---GWVFLYEDEFD-AALLTGVLDK 309
Cdd:cd03823   300 IQPgvnGLLFAPGDAEDlAAAMRRLLTD 327
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
125-273 2.33e-03

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: 38.92  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 125 WIDRLTRRWIRINATTPPRPPFTDTILHGHYRDWFASMEQGSTVPGRL---LHFGLIRPYKGVETLLEVMRGV--NDARL 199
Cdd:cd01635    63 PHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSLPLadkVSVGRLVPEKGIDLLLEALALLkaRLPDL 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015427105 200 SLRIVGNPATPQMRNLVEHACAQDPRISALLAYVEEPVLAREVSAAELVVLPYRQMHNSGTLLLALSLARPVLA 273
Cdd:cd01635   143 VLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIA 216
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
171-313 3.05e-03

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: 39.25  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 171 RLLHFGLIRPYKGVETLLEV---MRGVNDARLSLRIVGNPATpqmrNLVEHACAQDPRISALLAYVEEPVLAREVSAAEL 247
Cdd:cd03794   219 VVVYAGNIGKAQGLETLLEAaerLKRRPDIRFLFVGDGDEKE----RLKELAKARGLDNVTFLGRVPKEEVPELLSAADV 294
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015427105 248 VVLPYRQ----MHNSGT-LLLALSLARPVLAPWSESNAAIAEEVGPGWVFLYED--EFDAALLTGVLDKVRAA 313
Cdd:cd03794   295 GLVPLKDnpanRGSSPSkLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDpeALADAILELLDDPELRR 367
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
60-289 3.09e-03

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: 39.29  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105  60 RYDVLHLHWPeyllrhpTTAGTLAKQVCAAllllklqlTGTPVVRTLH--NLAPHEDRGWReRSLLRWIDRLTRRWIRI- 136
Cdd:cd03798    95 PPDLIHAHFA-------YPAGFAAALLARL--------YGVPYVVTEHgsDINVFPPRSLL-RKLLRWALRRAARVIAVs 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 137 --------NATTPPRPpfTDTILHGHYRDWFASMEQGSTVP--GRLLHF-GLIRPYKGVETLLEVMRGVNDAR--LSLRI 203
Cdd:cd03798   159 kalaeelvALGVPRDR--VDVIPNGVDPARFQPEDRGLGLPldAFVILFvGRLIPRKGIDLLLEAFARLAKARpdVVLLI 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015427105 204 VGNPATPQ-MRNLVEHACAQDPRIsaLLAYVEEPVLAREVSAAELVVLPYRQMHNSGTLLLALSLARPVLApwsESNAAI 282
Cdd:cd03798   237 VGDGPLREaLRALAEDLGLGDRVT--FTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVA---TDVGGI 311

                  ....*..
gi 1015427105 283 AEEVGPG 289
Cdd:cd03798   312 PEVVGDP 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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