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Conserved domains on  [gi|1622840893|ref|XP_028684335|]
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beta-1,4-galactosyltransferase 5 isoform X2 [Macaca mulatta]

Protein Classification

beta-1,4-galactosyltransferase( domain architecture ID 10097028)

beta-1,4-galactosyltransferase is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids

CAZY:  GT7
EC:  2.4.1.-
Gene Ontology:  GO:0016758
PubMed:  15465321
SCOP:  4000687

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 161-333 1.31e-114

Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen.


:

Pssm-ID: 132999 [Multi-domain]  Cd Length: 219  Bit Score: 331.08  E-value: 1.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 161 RWKVAILIPFRNRHEHLPVLFRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPE 240
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 241 SDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGD 320
Cdd:cd00899    81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                         170
                  ....*....|...
gi 1622840893 321 TGKYKSIPHHHRG 333
Cdd:cd00899   161 TGRYKMIRHIHDK 173
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 161-333 1.31e-114

Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen.


Pssm-ID: 132999 [Multi-domain]  Cd Length: 219  Bit Score: 331.08  E-value: 1.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 161 RWKVAILIPFRNRHEHLPVLFRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPE 240
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 241 SDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGD 320
Cdd:cd00899    81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                         170
                  ....*....|...
gi 1622840893 321 TGKYKSIPHHHRG 333
Cdd:cd00899   161 TGRYKMIRHIHDK 173
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 122-248 5.57e-77

N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 463972  Cd Length: 125  Bit Score: 231.96  E-value: 5.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 122 KGPIDINM-SEIGMDYIHElfsKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLIPMLQRQRLQFAFYVV 200
Cdd:pfam13733   1 VGPLKVNFnSPPTLEEVEK---KNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622840893 201 EQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGC 248
Cdd:pfam13733  78 EQAGNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
163-314 2.27e-06

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 47.68  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 163 KVAILIPFRNRHEHLpvlfRHLIPMLQRQ-RLQFAFYVVEQVGT---------------------QPFNRAMLFNVGFQE 220
Cdd:COG1216     4 KVSVVIPTYNRPELL----RRCLESLLAQtYPPFEVIVVDNGSTdgtaellaalafprvrvirnpENLGFAAARNLGLRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 221 AmkdlDWDCLIFHDVDHIPESDrnyygcgqmprhFATKLDKYMYLLpyteffggvsgLTVEQFRKINGFPNAFwGWGGED 300
Cdd:COG1216    80 A----GGDYLLFLDDDTVVEPD------------WLERLLAAACLL-----------IRREVFEEVGGFDERF-FLYGED 131

                         170
                  ....*....|....
gi 1622840893 301 DDLWNRVQNAGYSV 314
Cdd:COG1216   132 VDLCLRLRKAGYRI 145
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 161-333 1.31e-114

Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids; Beta-4-Galactosyltransferase transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues, hereby forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. At least seven homologous beta-4-galactosyltransferase isoforms have been identified that use different types of glycoproteins and glycolipids as substrates. Of the seven identified members of the beta-1,4-galactosyltransferase subfamily (beta1,4-Gal-T1 to -T7), b1,4-Gal-T1 is most characterized (biochemically). It is a Golgi-resident type II membrane enzyme with a cytoplasmic domain, membrane spanning region, and a stem region and catalytic domain facing the lumen.


Pssm-ID: 132999 [Multi-domain]  Cd Length: 219  Bit Score: 331.08  E-value: 1.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 161 RWKVAILIPFRNRHEHLPVLFRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPE 240
Cdd:cd00899     1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 241 SDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGD 320
Cdd:cd00899    81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                         170
                  ....*....|...
gi 1622840893 321 TGKYKSIPHHHRG 333
Cdd:cd00899   161 TGRYKMIRHIHDK 173
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 122-248 5.57e-77

N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 463972  Cd Length: 125  Bit Score: 231.96  E-value: 5.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 122 KGPIDINM-SEIGMDYIHElfsKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLIPMLQRQRLQFAFYVV 200
Cdd:pfam13733   1 VGPLKVNFnSPPTLEEVEK---KNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622840893 201 EQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGC 248
Cdd:pfam13733  78 EQAGNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 253-330 2.33e-34

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 120.79  E-value: 2.33e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840893 253 RHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHH 330
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYHK 78
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
163-314 2.27e-06

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 47.68  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 163 KVAILIPFRNRHEHLpvlfRHLIPMLQRQ-RLQFAFYVVEQVGT---------------------QPFNRAMLFNVGFQE 220
Cdd:COG1216     4 KVSVVIPTYNRPELL----RRCLESLLAQtYPPFEVIVVDNGSTdgtaellaalafprvrvirnpENLGFAAARNLGLRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 221 AmkdlDWDCLIFHDVDHIPESDrnyygcgqmprhFATKLDKYMYLLpyteffggvsgLTVEQFRKINGFPNAFwGWGGED 300
Cdd:COG1216    80 A----GGDYLLFLDDDTVVEPD------------WLERLLAAACLL-----------IRREVFEEVGGFDERF-FLYGED 131

                         170
                  ....*....|....
gi 1622840893 301 DDLWNRVQNAGYSV 314
Cdd:COG1216   132 VDLCLRLRKAGYRI 145
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 208-311 8.65e-05

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: 42.56  E-value: 8.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 208 FNRAMLFNVGFQEAMKD----LDWDCLIFHDV--DHIPESDRNYYGCGqmPRhfaTKLDKymyllPYTE--FFGGVSGLT 279
Cdd:cd06420    65 FRKAKIRNKAIAAAKGDylifIDGDCIPHPDFiaDHIELAEPGVFLSG--SR---VLLNE-----KLTErgIRGCNMSFW 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622840893 280 VEQFRKINGFPNAFWGWGGEDDDLWNRVQNAG 311
Cdd:cd06420   135 KKDLLAVNGFDEEFTGWGGEDSELVARLLNSG 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 147-314 1.07e-04

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: 43.58  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 147 IKLGGHWKPSDCMPRwkVAILIPFRNRHEHLPVLFRHLIPM--------------------------LQRQRLQFAFYVV 200
Cdd:COG1215    16 LALARRRRAPADLPR--VSVIIPAYNEEAVIEETLRSLLAQdypkeklevivvddgstdetaeiareLAAEYPRVRVIER 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840893 201 EQVGTQPFNRamlfNVGFQEAMKDLdwdcLIFHDVDHIPESDRnyygCGQMPRHFATkldkymyllPYTEFFGGVSGLTV 280
Cdd:COG1215    94 PENGGKAAAL----NAGLKAARGDI----VVFLDADTVLDPDW----LRRLVAAFAD---------PGVGASGANLAFRR 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622840893 281 EQFRKINGFPNAFWGwggEDDDLWNRVQNAGYSV 314
Cdd:COG1215   153 EALEEVGGFDEDTLG---EDLDLSLRLLRAGYRI 183
 
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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