NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15224178|ref|NP_180039|]
View 

Glycosyl transferase family 2 protein [Arabidopsis thaliana]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
227-463 1.30e-117

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06437:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 232  Bit Score: 351.61  E-value: 1.30e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDEVTKWSQkGVNIIYRHRLVRTGYKAGNL 306
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 307 KSAM-SCDYveayEFVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNG 385
Cdd:cd06437  80 AEGMkVAKG----EYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARS 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224178 386 VFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGP 463
Cdd:cd06437 155 STGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
227-463 1.30e-117

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 351.61  E-value: 1.30e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDEVTKWSQkGVNIIYRHRLVRTGYKAGNL 306
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 307 KSAM-SCDYveayEFVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNG 385
Cdd:cd06437  80 AEGMkVAKG----EYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARS 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224178 386 VFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGP 463
Cdd:cd06437 155 STGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
222-540 1.94e-40

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 150.28  E-value: 1.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 222 SGSEYPMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRdevtKWSQKGVNIIYRHRLVRTGy 301
Cdd:COG1215  24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIAR----ELAAEYPRVRVIERPENGG- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 302 KAGNLKSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKekpelglvqarwafvnkDENLltrlqninlcfhfeveq 381
Cdd:COG1215  99 KAAALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-----------------DPGV----------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 382 qvngvflnffGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHS 461
Cdd:COG1215 142 ----------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224178 462 GPMQLFRLCLRSILTSKIAMWkkANLILLFFLLRKLILPFYSFTLFCVILPITMFVPEAELPIWVICYVPIFMSLLNIL 540
Cdd:COG1215 212 GGLQLLLKHRPLLRPRRLLLF--LLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
224-469 1.29e-21

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 100.10  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  224 SEYPMVLVQIPMCNER-EVYEQSISAVCQLDWPKDRLLVQVLDDSDdesiqeliRDEVTKWSQK-GVNIIyrhrlVRTGY 301
Cdd:PRK11498 257 SLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGG--------REEFRQFAQEvGVKYI-----ARPTH 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  302 ---KAGNLKSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKD---ENL--LTRLQNINL 373
Cdd:PRK11498 324 ehaKAGNINNALK---YAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGT 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  374 CFHFEVeQQVNGVFLNFFgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYK 453
Cdd:PRK11498 401 LFYGLV-QDGNDMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHI 478
                        250
                 ....*....|....*.
gi 15224178  454 KQQHRWHSGPMQLFRL 469
Cdd:PRK11498 479 GQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
320-516 4.14e-16

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 76.99  E-value: 4.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   320 FVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQArWAFVNKDENLLTRLQninlCFHFEVEQQVNGVFLNFFG----FNG 395
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQG-PILPMNVGNYLEELA----ALFFADDHGKSIPVRMALGrvlpFVG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   396 TAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWhsgpmqlFRLCLRSIL 475
Cdd:pfam13632  75 SGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRW-------AYGCLLILL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 15224178   476 TSKIAMWKKANLILLFFLLRKLILPFYSFTLFCVILPITMF 516
Cdd:pfam13632 148 IRLLGYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALLA 188
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
227-463 1.30e-117

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 351.61  E-value: 1.30e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDEVTKWSQkGVNIIYRHRLVRTGYKAGNL 306
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 307 KSAM-SCDYveayEFVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNG 385
Cdd:cd06437  80 AEGMkVAKG----EYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARS 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224178 386 VFLNFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGP 463
Cdd:cd06437 155 STGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
227-467 1.34e-56

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 192.02  E-value: 1.34e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNE-REVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDEVTKWsqkgvNIIYRHRLVRTGYKAGN 305
Cdd:cd06421   1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEY-----GYRYLTRPDNRHAKAGN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 306 LKSAMscDYVEaYEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKDENLLT--RLQNINLCFHFEVEQQV 383
Cdd:cd06421  76 LNNAL--AHTT-GDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLadGAPNEQELFYGVIQPGR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 384 NGVFLNFFGfnGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGP 463
Cdd:cd06421 153 DRWGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230

                ....
gi 15224178 464 MQLF 467
Cdd:cd06421 231 LQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
222-540 1.94e-40

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 150.28  E-value: 1.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 222 SGSEYPMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRdevtKWSQKGVNIIYRHRLVRTGy 301
Cdd:COG1215  24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIAR----ELAAEYPRVRVIERPENGG- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 302 KAGNLKSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKekpelglvqarwafvnkDENLltrlqninlcfhfeveq 381
Cdd:COG1215  99 KAAALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-----------------DPGV----------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 382 qvngvflnffGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHS 461
Cdd:COG1215 142 ----------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224178 462 GPMQLFRLCLRSILTSKIAMWkkANLILLFFLLRKLILPFYSFTLFCVILPITMFVPEAELPIWVICYVPIFMSLLNIL 540
Cdd:COG1215 212 GGLQLLLKHRPLLRPRRLLLF--LLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
231-468 2.41e-34

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 130.98  E-value: 2.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 231 VQIPMCNER-EVYEQSISAVCQLDWPKDRLLVqVLDDSDDESIQELIRDEVtkwSQKGVNIIYRHRLVRTGYKAGNLKSA 309
Cdd:cd06435   2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIV-IDNNTKDEALWKPVEAHC---AQLGERFRFFHVEPLPGAKAGALNYA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 310 MSCDYVEAyEFVAIFDADFQPNSDFLKLTVPHFkEKPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQ----QVNG 385
Cdd:cd06435  78 LERTAPDA-EIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMvsrnERNA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 386 VFlnffgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWHSGPMQ 465
Cdd:cd06435 156 II-----QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQ 230

                ...
gi 15224178 466 LFR 468
Cdd:cd06435 231 ILK 233
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
231-419 2.70e-34

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 128.88  E-value: 2.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 231 VQIPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESIQELIRdevtkWSQKGVNIIYRHRLVRTGYKAGNLKSAM 310
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTLEILEE-----LAALYIRRVLVVRDKENGGKAGALNAGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 311 S-CDYveayEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLN 389
Cdd:cd06423  75 RhAKG----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGG 150
                       170       180       190
                ....*....|....*....|....*....|
gi 15224178 390 FFGFNGTAGVWRIKALEESGGWLERTTVED 419
Cdd:cd06423 151 VLVLSGAFGAFRREALREVGGWDEDTLTED 180
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
227-465 3.54e-28

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 113.50  E-value: 3.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDDSDDESIQELIRDevTKWSQKGVNIIYRHRLVRTGYKAgnl 306
Cdd:cd06427   1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARA--LRLPSIFRVVVVPPSQPRTKPKA--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 307 ksamsCDYVEAY---EFVAIFDADFQPNSDFLKLTVPHF-KEKPELGLVQARWAFVNKDENLLTRLQNINLCFHFEveqq 382
Cdd:cd06427  76 -----CNYALAFargEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFD---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 383 vngVFLNFFG-------FNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVkVLCEVPESYEAYKKQ 455
Cdd:cd06427 147 ---YLLPGLArlglpipLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNST-TLEEANNALGNWIRQ 222
                       250
                ....*....|
gi 15224178 456 QHRWHSGPMQ 465
Cdd:cd06427 223 RSRWIKGYMQ 232
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
224-469 1.29e-21

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 100.10  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  224 SEYPMVLVQIPMCNER-EVYEQSISAVCQLDWPKDRLLVQVLDDSDdesiqeliRDEVTKWSQK-GVNIIyrhrlVRTGY 301
Cdd:PRK11498 257 SLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGG--------REEFRQFAQEvGVKYI-----ARPTH 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  302 ---KAGNLKSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKD---ENL--LTRLQNINL 373
Cdd:PRK11498 324 ehaKAGNINNALK---YAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGT 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  374 CFHFEVeQQVNGVFLNFFgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYK 453
Cdd:PRK11498 401 LFYGLV-QDGNDMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHI 478
                        250
                 ....*....|....*.
gi 15224178  454 KQQHRWHSGPMQLFRL 469
Cdd:PRK11498 479 GQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
320-516 4.14e-16

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 76.99  E-value: 4.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   320 FVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQArWAFVNKDENLLTRLQninlCFHFEVEQQVNGVFLNFFG----FNG 395
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQG-PILPMNVGNYLEELA----ALFFADDHGKSIPVRMALGrvlpFVG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   396 TAGVWRIKALEESGGWLERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRWhsgpmqlFRLCLRSIL 475
Cdd:pfam13632  75 SGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRW-------AYGCLLILL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 15224178   476 TSKIAMWKKANLILLFFLLRKLILPFYSFTLFCVILPITMF 516
Cdd:pfam13632 148 IRLLGYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALLA 188
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
233-407 3.57e-13

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 67.81  E-value: 3.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   233 IPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESiqeliRDEVTKWSQKGVNIIYRHRLVRTGyKAGNLKSAMSc 312
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTDGT-----VEIAEEYAKKDPRVRVIRLPENRG-KAGARNAGLR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   313 dyvEAY-EFVAIFDADFQPNSDFLKLTVPHFkEKPELGLVQARWAFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFF 391
Cdd:pfam00535  76 ---AATgDYIAFLDADDEVPPDWLEKLVEAL-EEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPF 151
                         170
                  ....*....|....*.
gi 15224178   392 GFNGTAGVWRiKALEE 407
Cdd:pfam00535 152 LIGGFALYRR-EALEE 166
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
227-459 7.24e-11

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 62.77  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESIqELIRDEVTKWSQKGVNIIYRHRLVRTGYKAGNL 306
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVV-VVNPSDAETL-DVAEEIAARFPDVRLRVIRNARLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   307 KSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQARwAFVNKDENLLTRLQninlCFHFEVEQQVNGV 386
Cdd:pfam13641  80 NHGFR---AVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALG----ALEFALRHLRMMS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224178   387 FLNFFGF---NGTAGVWRIKALEESGGWLERTTV-EDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHRW 459
Cdd:pfam13641 151 LRLALGVlplSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARW 227
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
227-437 6.30e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 59.33  E-value: 6.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESiQELIRdevtKWSQKGVNIIYRHRLVRTGyKAGNL 306
Cdd:COG0463   2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDGT-AEILR----ELAAKDPRIRVIRLERNRG-KGAAR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 307 KSAMScdyvEA-YEFVAIFDADFQPNSDFLKLTVPHFKEKPElGLVQARWaFVNKDENLLTRLQNINLCFHfeveqqvnG 385
Cdd:COG0463  75 NAGLA----AArGDYIAFLDADDQLDPEKLEELVAALEEGPA-DLVYGSR-LIREGESDLRRLGSRLFNLV--------R 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15224178 386 VFLNFFGFNGTAGVWRIKALEESGgwLERTTVEDMDIaVRAHLHGWKFIYLN 437
Cdd:COG0463 141 LLTNLPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
193-458 7.38e-10

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 59.90  E-value: 7.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 193 LCLGCLWIKFKKIKPRIDEEHfrnddfegsgseYPMVLVQIPMCNEREVYEQSISAVCQLDWPKDRL--LVqVLDDSDDE 270
Cdd:cd06439   7 LLLKLLARLRPKPPSLPDPAY------------LPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLeiIV-VSDGSTDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 271 SiQELIRDevtkWSQKGVNIIYRHRlvRTGyKAGNLKSAMScdYVEAyEFVAIFDADFQPNSDFLKLTVPHFKEkPELGL 350
Cdd:cd06439  74 T-AEIARE----YADKGVKLLRFPE--RRG-KAAALNRALA--LATG-EIVVFTDANALLDPDALRLLVRHFAD-PSVGA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 351 VQARWAFVNKD-----ENLLTRLQNiNLCFHfevEQQVNGVflnfFGFNGTagvwrIKAL--EESGGWLERTTVEDMDIA 423
Cdd:cd06439 142 VSGELVIVDGGgsgsgEGLYWKYEN-WLKRA---ESRLGST----VGANGA-----IYAIrrELFRPLPADTINDDFVLP 208
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15224178 424 VRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQHR 458
Cdd:cd06439 209 LRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVR 243
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
233-358 1.05e-07

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 51.74  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 233 IPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESIQELIRdevtkwSQKGVNIIYRHRLVRTGYKAGNLKSAMSc 312
Cdd:cd00761   3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEILEE------YAKKDPRVIRVINEENQGLAAARNAGLK- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15224178 313 dyvEA-YEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFV 358
Cdd:cd00761  75 ---AArGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
300-459 2.54e-07

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 51.13  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   300 GYKAGNLKSAMScdyVEAYEFVAIFDADFQPNSDFLKLTVPHFKEkPELGLVQArWAFVNKDENLLTRLQNINLCFHfev 379
Cdd:pfam13506  16 NPKVNNLLQGLE---AAKYDLLVISDSDIRVPPDYLRDLLAPLAD-PKVGLVTS-PPVGSDPKGLAAALEAAFFNTL--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178   380 eqqvNGVFLNFFGFNGTA-G---VWRIKALEESGGW--LERTTVEDMDIAVRAHLHGWKFIYLNDVKVLCEVPE--SYEA 451
Cdd:pfam13506  88 ----AGVLQAALSGIGFAvGmsmAFRRADLERIGGFeaLADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRA 163

                  ....*...
gi 15224178   452 YKKQQHRW 459
Cdd:pfam13506 164 FMARQLRW 171
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
227-472 8.66e-07

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 49.99  E-value: 8.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 227 PMVLVQIPMCNEREVYEQSISAVCQLDWPKDRLLVqVLDDSDDESiqeliRDEVTKWSQKGVNIIYRHRlvRTGYKAGN- 305
Cdd:COG1216   3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDGT-----AELLAALAFPRVRVIRNPE--NLGFAAARn 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 306 --LKSAmscdyveAYEFVAIFDADfqpnsdflklTVPHfkekpelglvqarwafvnkdENLLTRLqninlcfhfeveqqv 383
Cdd:COG1216  75 lgLRAA-------GGDYLLFLDDD----------TVVE--------------------PDWLERL--------------- 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 384 ngvfLNFFGFngtagVWRIKALEESGGWLERTTV--EDMDIAVRAHLHGWKFIYLNDVKVLCEVPESYEAYKKQQH---- 457
Cdd:COG1216 103 ----LAAACL-----LIRREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYlgrn 173
                       250       260
                ....*....|....*....|
gi 15224178 458 -----RWHSGPMQLFRLCLR 472
Cdd:COG1216 174 rllflRKHGPRPLLRLALLR 193
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
231-371 2.40e-06

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 48.53  E-value: 2.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 231 VQIPMCNEREVYEQSISAVCQLDwpkDRLLVQVLDD-SDDESIQeLIRDEVTkwsQKGVNIIYRHRL-VRTG------YK 302
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLLRNK---PNFLVLVIDDaSDDDTAG-IVRLAIT---DSRVHLLRRHLPnARTGkgdalnAA 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 303 AGNLKSAMSCDYVEAY-EFVAIFDADFQPNSDFLKLTVPHFkEKPELGLVQARWAFVNKDENLLTRLQNI 371
Cdd:cd06436  74 YDQIRQILIEEGADPErVIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDL 142
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
234-369 1.41e-05

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 47.27  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 234 PMCNE--REVYE--QSISAVCQLDWPKDRLLVQVLDDSDDESI---QELIRDEVTKWSQKGVNIIYRHRLVRTGYKAGNL 306
Cdd:cd04191   6 PVYNEdpARVFAglRAMYESLAKTGLADHFDFFILSDTRDPDIwlaEEAAWLDLCEELGAQGRIYYRRRRENTGRKAGNI 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224178 307 KsamscDYVE----AYEFVAIFDADFQPNSDFLKLTVPHFKEKPELGLVQARWAFVNKdENLLTRLQ 369
Cdd:cd04191  86 A-----DFCRrwgsRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGA-ETLFARLQ 146
MdoH COG2943
Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport ...
263-327 4.62e-04

Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport and metabolism];


Pssm-ID: 442186 [Multi-domain]  Cd Length: 661  Bit Score: 43.32  E-value: 4.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15224178 263 VLDDSDDESIqelIRDEVTKWSQ------KGVNIIYRHRLVRTGYKAGNLKsamscDYVE----AYEFVAIFDAD 327
Cdd:COG2943 136 ILSDTTDPDI---WAAEEAAWAAlrarlgGGGRIFYRRRRRNTGRKAGNIA-----DFCRrwggAYDYMLVLDAD 202
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
234-327 6.56e-04

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 42.95  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178  234 PMCNE---------REVYEqSISAVCQLDwpkdRLLVQVLDDSDDESI---QELIRDEVTKWSQKGVNIIYRHRLVRTGY 301
Cdd:PRK05454 131 PIYNEdparvfaglRAMYE-SLAATGHGA----HFDFFILSDTRDPDIaaaEEAAWLELRAELGGEGRIFYRRRRRNVGR 205
                         90       100       110
                 ....*....|....*....|....*....|
gi 15224178  302 KAGNLKsamscDYVE----AYEFVAIFDAD 327
Cdd:PRK05454 206 KAGNIA-----DFCRrwggAYDYMVVLDAD 230
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
231-462 3.96e-03

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 39.58  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 231 VQIPMCNEREVYEQSISAVCQLDWPKDRLLVQVLDD-SDDES--IQELIRDEvtkwSQKGVNIIYRHRLVRTGYKAGnLK 307
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDhSTDGTvqILEFAAAK----PNFQLKILNNSRVSISGKKNA-LT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 308 SAMScdyVEAYEFVAIFDADFQPNSDFLKLTV-PHFKEKPelGLVQARWAFVnKDENLLTRLQNINLCFhfeveqqVNGV 386
Cdd:cd04192  76 TAIK---AAKGDWIVTTDADCVVPSNWLLTFVaFIQKEQI--GLVAGPVIYF-KGKSLLAKFQRLDWLS-------LLGL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224178 387 FLNFFGF------NGTAGVWRIKALEESGGW--LERTTVEDMDIAVRAHLHGW-KFIYL--NDVKVLCEVPESYEAYKKQ 455
Cdd:cd04192 143 IAGSFGLgkpfmcNGANMAYRKEAFFEVGGFegNDHIASGDDELLLAKVASKYpKVAYLknPEALVTTQPVTSWKELLNQ 222

                ....*..
gi 15224178 456 QHRWHSG 462
Cdd:cd04192 223 RKRWASK 229
 
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