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Conserved domains on  [gi|447213309|ref|WP_001290565|]
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MULTISPECIES: glycosyltransferase family 2 protein, partial [Enterobacteriaceae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 9-188 3.20e-42

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 146.77  E-value: 3.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATG 88
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVICRsqsfdpalqvyapmpWSVRQELLPDLKFFSSQDIPSDFFRTFVWW 168
Cdd:COG0463   84 DYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS---------------RLIREGESDLRRLGSRLFNLVRLLTNLPDS 148

                        170       180
                 ....*....|....*....|.
gi 447213309 169 -PWDKLLRRQFItsHQLRFQE 188
Cdd:COG0463  149 tSGFRLFRREVL--EELGFDE 167
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 9-188 3.20e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 146.77  E-value: 3.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATG 88
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVICRsqsfdpalqvyapmpWSVRQELLPDLKFFSSQDIPSDFFRTFVWW 168
Cdd:COG0463   84 DYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS---------------RLIREGESDLRRLGSRLFNLVRLLTNLPDS 148

                        170       180
                 ....*....|....*....|.
gi 447213309 169 -PWDKLLRRQFItsHQLRFQE 188
Cdd:COG0463  149 tSGFRLFRREVL--EELGFDE 167
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 10-162 1.56e-39

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: 138.30  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   10 SVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATGE 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447213309   90 YVIFLDDDDYVDNMMLERMYARASDIQADVVIC----RSQSFDPALQVYAPMPWSVRQELLPDLKFFSSQDIPSDFF 162
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsryvIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 11-127 5.76e-33

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: 120.69  E-value: 5.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATGEY 90
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447213309  91 VIFLDDDDYVDNMMLERMYARA-SDIQADVVICRSQSF 127
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELlADPEADAVGGPGNLL 118
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 9-231 2.39e-24

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 102.05  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNtTNLGGGGSRNIGLDAATG 88
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ-ANAGVSVARNTGLAVATG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVICRSQsfdpalqvyapmpWSVRQellpdlKFFSSQDIPSDFFRT---- 164
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNAD-------------WCFRD------TGETWQSIPSDRLRStgvl 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309 165 --------------FVWWPWDKLLRRQFITSHQLRFQEIRTTNDLFFVCAFMLMANRISVLNETLISHTINrSESLSATR 230
Cdd:PRK10073 148 sgpdwlrmalssrrWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLH-DTSVSRLP 226


                 .
gi 447213309 231 A 231
Cdd:PRK10073 227 R 227
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 9-94 3.16e-09

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.75  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309    9 VSVIIPVHNAAGYISDTLSTvLSQTLNDIEIIIVNDCSDDNTLEIVSALAetdsrIRVInnTTNLGGGGSRNIGLDAATG 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIARSLG-----AKVI--HSPKGRARQMNAGAALAKG 72


                  ....*.
gi 447213309   89 EYVIFL 94
Cdd:TIGR04283  73 DILLFL 78
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-99 4.14e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 47.87  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHNAAGYISDTLSTVLSQT-LNDI--EIIIVNDCSDDNTLEIVSALAET---DSRIRVINNtTNLGGGGSRNIGL 83
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSQIgTESLswEIIVVDNNSTDNTAQVVQEYQKNwpsPYPLRYCFE-PQQGAAFARQRAI 82

                         90
                 ....*....|....*.
gi 447213309  84 DAATGEYVIFLDDDDY 99
Cdd:NF038302  83 QEAKGELIGFLDDDNL 98
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 9-188 3.20e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 146.77  E-value: 3.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATG 88
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVICRsqsfdpalqvyapmpWSVRQELLPDLKFFSSQDIPSDFFRTFVWW 168
Cdd:COG0463   84 DYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS---------------RLIREGESDLRRLGSRLFNLVRLLTNLPDS 148

                        170       180
                 ....*....|....*....|.
gi 447213309 169 -PWDKLLRRQFItsHQLRFQE 188
Cdd:COG0463  149 tSGFRLFRREVL--EELGFDE 167
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 10-162 1.56e-39

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: 138.30  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   10 SVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATGE 89
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447213309   90 YVIFLDDDDYVDNMMLERMYARASDIQADVVIC----RSQSFDPALQVYAPMPWSVRQELLPDLKFFSSQDIPSDFF 162
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsryvIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 11-127 5.76e-33

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: 120.69  E-value: 5.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATGEY 90
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447213309  91 VIFLDDDDYVDNMMLERMYARA-SDIQADVVICRSQSF 127
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELlADPEADAVGGPGNLL 118
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
9-113 1.80e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 112.78  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAetDSRIRVINNTTNLGGGGSRNIGLDAATG 88
Cdd:COG1216    5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGLRAAGG 82

                         90       100
                 ....*....|....*....|....*
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARAS 113
Cdd:COG1216   83 DYLLFLDDDTVVEPDWLERLLAAAC 107
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-120 5.41e-28

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: 111.76  E-value: 5.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQT--LNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAA 86
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAA 110

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447213309  87 TGEYVIFLDDDDYVDNMMLERMYARASDIQADVV 120
Cdd:COG1215  111 RGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 11-121 1.72e-24

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 98.80  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLS--QTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATG 88
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVI 121
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 9-231 2.39e-24

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 102.05  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNtTNLGGGGSRNIGLDAATG 88
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ-ANAGVSVARNTGLAVATG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADVVICRSQsfdpalqvyapmpWSVRQellpdlKFFSSQDIPSDFFRT---- 164
Cdd:PRK10073  87 KYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNAD-------------WCFRD------TGETWQSIPSDRLRStgvl 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309 165 --------------FVWWPWDKLLRRQFITSHQLRFQEIRTTNDLFFVCAFMLMANRISVLNETLISHTINrSESLSATR 230
Cdd:PRK10073 148 sgpdwlrmalssrrWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLH-DTSVSRLP 226


                 .
gi 447213309 231 A 231
Cdd:PRK10073 227 R 227
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 11-126 1.27e-21

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 91.00  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDT---LSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLggGGSRNI--GLDA 85
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNF--GQQAALlaGLDH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447213309  86 ATGEYVIFLDDDDYVDNMMLERMYARASDiQADVVICRSQS 126
Cdd:cd04187   79 ARGDAVITMDADLQDPPELIPEMLAKWEE-GYDVVYGVRKN 118
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 9-121 1.66e-21

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 92.29  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQT--LNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGsRNIGLDAA 86
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAG-LNIGIRNS 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447213309  87 TGEYVIFLDDDDYVDNMMLERMYARASDIQADVVI 121
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVG 115
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 11-134 6.36e-21

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: 89.21  E-value: 6.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALA-ETDSRIRVINNTTNLGGGGSRNIGLDAATGE 89
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAaLYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447213309  90 YVIFLDDDDYVDNMMLERMYARA-SDIQADVV------ICRSQSFDPALQVY 134
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFfADPKVGAVqgrvrvRNGSENLLTRLQAI 132
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 10-167 1.29e-19

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 86.06  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAetDSRIRVInnttnlggggSR---------N 80
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYE--DKITYWI----------SEpdkgiydamN 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  81 IGLDAATGEYVIFL-DDDDYVDNMMLERMYARASDIQADVVICRSQSFDPALQVyaPMPWSVRQELLPDLKFFSSQDIPS 159
Cdd:cd06433   69 KGIALATGDIIGFLnSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRV--IGRRRPPPFLDKFLLYGMPICHQA 146


                 ....*...
gi 447213309 160 DFFRTFVW 167
Cdd:cd06433  147 TFFRRSLF 154
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-112 6.19e-19

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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 82.99  E-value: 6.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIvsaLAETDSRIRVINNTTNLGGGGSRNIGLDAATGEY 90
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVEL---LRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100
                 ....*....|....*....|..
gi 447213309  91 VIFLDDDDYVDNMMLERMYARA 112
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAA 99
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-167 1.54e-18

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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 83.45  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVI-NNTTNLGGGGSRNIGLDAATG 88
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILiRNGKNLGVARNFESLLQAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQ-ADVVICRSQSFDPALQVYAPMPWSVRqellpdlKFFSSQDIPSDFFRTFVW 167
Cdd:cd04196   81 DYVFFCDQDDIWLPDKLERLLKAFLKDDkPLLVYSDLELVDENGNPIGESFFEYQ-------KIKPGTSFNNLLFQNVVT 153
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 9-99 9.93e-18

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 80.71  E-value: 9.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAA-GYISDTLSTVLSQTLNDIEIIIVNDCSDDN-TLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAA 86
Cdd:cd04184    3 ISIVMPVYNTPeKYLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPRIKVVFREENGGISAATNSALELA 82

                         90
                 ....*....|...
gi 447213309  87 TGEYVIFLDDDDY 99
Cdd:cd04184   83 TGEFVALLDHDDE 95
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 8-130 2.52e-15

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: 74.93  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   8 AVSVIIPVHNAAGYISDTLSTVLSQT--LNDIEIIIVNDCSDDNTLEIVSALAetDSRIRVINNTTNLGGGGSRNIGLDA 85
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGSTDGTAEIAREYA--DKGVKLLRFPERRGKAAALNRALAL 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447213309  86 ATGEYVIFLDDDDYVDNMMLERMYARASDIQADVVICRSQSFDPA 130
Cdd:cd06439  108 ATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGG 152
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 11-121 2.57e-13

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 68.36  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSqTLN-----DIEIIIVNDCSDDNTLEIVSALAET-DSRIRVINNTTNLGGGGSRNIGLD 84
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVE-YLEerpsfSYEIIVVDDGSKDGTAEVARKLARKnPALIRVLTLPKNRGKGGAVRAGML 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447213309  85 AATGEYVIFLDDDDYVDNMMLERMYARASDIQADVVI 121
Cdd:cd04188   80 AARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 11-121 2.17e-12

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 66.02  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLN-DIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAATGE 89
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447213309  90 YVIFLDDDDYVDNMMLERMYARASDIQADVVI 121
Cdd:cd06442   81 VIVVMDADLSHPPEYIPELLEAQLEGGADLVI 112
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 9-94 4.99e-12

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 64.90  E-value: 4.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVnDC-SDDNTLEIVSALAetdsrIRVInnTTNLGGGGSRNIGLDAAT 87
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVV-DGgSTDGTVAIARSAG-----VVVI--SSPKGRARQMNAGAAAAR 72


                 ....*..
gi 447213309  88 GEYVIFL 94
Cdd:cd02522   73 GDWLLFL 79
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 11-125 4.91e-11

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 62.09  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQT-LNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVI------NNTTNLGGGGSRNIGL 83
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDfEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIvlvgshNSPSPKGVGYAKNQAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447213309  84 DAATGEYVIFLDDDDYVDNMMLERMYARASDIQADVVICRSQ 125
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVR 122
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 10-95 1.71e-10

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 61.45  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHN-AAGYISDTLSTVLSQT----LndIEIIIVNDCSDDNTLEIvsALAETDSR----IRVINNTTNLGGGGSRN 80
Cdd:cd02510    1 SVIIIFHNeALSTLLRTVHSVINRTppelL--KEIILVDDFSDKPELKL--LLEEYYKKylpkVKVLRLKKREGLIRARI 76

                         90
                 ....*....|....*
gi 447213309  81 IGLDAATGEYVIFLD 95
Cdd:cd02510   77 AGARAATGDVLVFLD 91
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 9-119 2.11e-10

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 60.38  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVlsQTLNDiEIIIVNDCSDDNTLEIvsALAETDsriRVINNtTNLGGGGSRNIGLDAATG 88
Cdd:cd02511    2 LSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDRTVEI--AKEYGA---KVYQR-WWDGFGAQRNFALELATN 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447213309  89 EYVIFLDDDDYVDNMMLERMYARASDIQADV 119
Cdd:cd02511   73 DWVLSLDADERLTPELADEILALLATDDYDG 103
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 10-108 2.59e-10

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 60.75  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   10 SVIIPVHNAAG--YISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVIN-NTTNLGGGGSRNIGLDAA 86
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNaPDTTYSLAASRNRGTSHA 80

                          90       100
                  ....*....|....*....|..
gi 447213309   87 TGEYVIFLDDDDYVDNMMLERM 108
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQ 102
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 6-108 4.13e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 60.55  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   6 SIAVSVIIPVHNAAGYISDTLSTVLSQTLNDI--------EIIIVNDCSDDNTLEIVSALAE----TDSRIRVINNTTNL 73
Cdd:PTZ00260  69 DVDLSIVIPAYNEEDRLPKMLKETIKYLESRSrkdpkfkyEIIIVNDGSKDKTLKVAKDFWRqninPNIDIRLLSLLRNK 148

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447213309  74 GGGGSRNIGLDAATGEYVIFLDDDDYVDNMMLERM 108
Cdd:PTZ00260 149 GKGGAVRIGMLASRGKYILMVDADGATDIDDFDKL 183
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 4-120 5.46e-10

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 59.33  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   4 KESIAVSVIIPVHNAAGYISdTLSTVLSQTLNDI---EIIIVNDCSDDNTLEIVSALAET--DSRIRVINNTTNLGGGGS 78
Cdd:PLN02726   6 EGAMKYSIIVPTYNERLNIA-LIVYLIFKALQDVkdfEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447213309  79 RNIGLDAATGEYVIFLDDD-----DYVDNMMlermyARASDIQADVV 120
Cdd:PLN02726  85 YIHGLKHASGDFVVIMDADlshhpKYLPSFI-----KKQRETGADIV 126
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
9-170 1.48e-09

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 58.47  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSD--DNTLEIVSALaeTDSRIRVINNTTNLGGGGSRNIGLDAA 86
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTswEQLQQYVTAL--NDPRITYIHNDINSGACAVRNQAIMLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  87 TGEYVIFLDDDD-YVDNMM------LERMYARASdIQADVVICRSQSFD-PA-LQVYAPMPWSVRqellpdlKFFSSQDI 157
Cdd:PRK10018  85 QGEYITGIDDDDeWTPNRLsvflahKQQLVTHAF-LYANDYVCQGEVYSqPAsLPLYPKSPYSRR-------LFYKRNII 156

                        170
                 ....*....|...
gi 447213309 158 PSDFFRtfvwWPW 170
Cdd:PRK10018 157 GNQVFT----WAW 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 9-94 3.16e-09

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.75  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309    9 VSVIIPVHNAAGYISDTLSTvLSQTLNDIEIIIVNDCSDDNTLEIVSALAetdsrIRVInnTTNLGGGGSRNIGLDAATG 88
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIARSLG-----AKVI--HSPKGRARQMNAGAALAKG 72


                  ....*.
gi 447213309   89 EYVIFL 94
Cdd:TIGR04283  73 DILLFL 78
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 9-120 6.53e-09

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: 55.84  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309    9 VSVIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAE--TDSRIRVINNTTNLGGGG---SRNIGL 83
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAArfPDVRLRVIRNARLLGPTGksrGLNHGF 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 447213309   84 DAATGEYVIFLDDDDYVDNMMLERMYARASDIQADVV 120
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAV 120
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-132 1.46e-08

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: 54.60  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLND--IEIIIVNDCSDDNTLEIVS-ALAETDSRIRVINNTTNLGGGGSRNI--GLDA 85
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNNSRVSISGKKNALttAIKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447213309  86 ATGEYVIFLDDDDYV-DNMMLERMYARASDIQADV---VIC-RSQSFDPALQ 132
Cdd:cd04192   81 AKGDWIVTTDADCVVpSNWLLTFVAFIQKEQIGLVagpVIYfKGKSLLAKFQ 132
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 25-101 1.26e-07

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 51.48  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  25 TLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDsRIRVINNTTNLGGGGSRNIGLDAATGE---YVIFLDDDDYVD 101
Cdd:cd04185   15 CLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLD-NIVYLRLPENLGGAGGFYEGVRRAYELgydWIWLMDDDAIPD 93
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 9-110 5.65e-07

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 49.95  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAAG-YISDTLSTVLSQTlnDIEIIIVNDCSDDNTLEIVSALaETDSRIRVINNTTnlggGGSRN---IGLD 84
Cdd:cd06434    2 VTVIIPVYDEDPdVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILSQT-VKYGGIFVITVPH----PGKRRalaEGIR 74

                         90       100
                 ....*....|....*....|....*.
gi 447213309  85 AATGEYVIFLDDDDYVDNMMLERMYA 110
Cdd:cd06434   75 HVTTDIVVLLDSDTVWPPNALPEMLK 100
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 11-97 1.44e-06

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 47.96  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAEtDSRIRVI-----NNTTNLGGggSRNIGLDA 85
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKS-QFPIPIKhvwqeDEGFRKAK--IRNKAIAA 77

                         90
                 ....*....|..
gi 447213309  86 ATGEYVIFLDDD 97
Cdd:cd06420   78 AKGDYLIFIDGD 89
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-99 4.14e-06

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 47.87  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHNAAGYISDTLSTVLSQT-LNDI--EIIIVNDCSDDNTLEIVSALAET---DSRIRVINNtTNLGGGGSRNIGL 83
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSQIgTESLswEIIVVDNNSTDNTAQVVQEYQKNwpsPYPLRYCFE-PQQGAAFARQRAI 82

                         90
                 ....*....|....*.
gi 447213309  84 DAATGEYVIFLDDDDY 99
Cdd:NF038302  83 QEAKGELIGFLDDDNL 98
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 9-97 8.17e-05

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 43.96  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309   9 VSVIIPVHNAagyiSDTLSTVLSQTL-------NDIEIIIVNDCSDDNTLEIVSALAET-DSRIRVINNTTNLGGGGSRN 80
Cdd:PRK10714   8 VSVVIPVYNE----QESLPELIRRTTaaceslgKEYEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIM 83

                         90
                 ....*....|....*..
gi 447213309  81 IGLDAATGEYVIFLDDD 97
Cdd:PRK10714  84 AGFSHVTGDLIITLDAD 100
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 11-67 1.77e-04

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: 41.99  E-value: 1.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQTLNdIEIIIVNDCSDDNTLEIVSaLAETDSRIRVI 67
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPN-FLVLVIDDASDDDTAGIVR-LAITDSRVHLL 55
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 10-98 1.06e-03

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 39.99  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  10 SVIIPVHN--AAGYISDTLSTVLSQTLNDIEIIIVNDCSDDNTLEIVSALAETDSRIRVINNTTNLGGGGSRNIGLDAAT 87
Cdd:cd04195    1 SVLMSVYIkeKPEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                         90
                 ....*....|.
gi 447213309  88 GEYVIFLDDDD 98
Cdd:cd04195   81 YDWVARMDTDD 91
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 11-120 5.51e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 37.58  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  11 VIIPVHNAAGYISDTLSTVLSQT--LNDIEIIIVNDCSDDNTLEIVSALAETdsrirVI--NNTTNLGGG-----GSRNI 81
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDypRELYRIFVVADNCTDDTAQVARAAGAT-----VLerHDPERRGKGyaldfGFRHL 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447213309  82 GLDAATGEYVIFLDDDDYVDNMMLERMyARASDIQADVV 120
Cdd:cd06438   76 LNLADDPDAVVVFDADNLVDPNALEEL-NARFAAGARVV 113
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 22-111 6.72e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 37.65  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213309  22 ISDTLSTVLSQTLNDIEIIIVndcsdDNTLEIVSALAETD--SRIRVINNTTNLGGGGSRNIGLDAATG---EYVIFLDD 96
Cdd:cd02526   10 LSKLKELLAALAEQVDKVVVV-----DNSSGNDIELRLRLnsEKIELIHLGENLGIAKALNIGIKAALEngaDYVLLFDQ 84

                         90
                 ....*....|....*
gi 447213309  97 DDYVDNMMLERMYAR 111
Cdd:cd02526   85 DSVPPPDMVEKLLAY 99
 
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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