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Conserved domains on  [gi|1034643452|ref|XP_016864488|]
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beta-1,4-galactosyltransferase 7 isoform X1 [Homo sapiens]

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 ...
 1-201 1.64e-99

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: 287.56  E-value: 1.64e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452   1 MRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSN--STDYIAMHDVDLLPLNEELDYGFPEaGPFHVASPE--L 76
Cdd:cd00899    24 LHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKdgDWDCFIFHDVDLLPENDRNLYGCEE-GPRHLSVPLdkF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452  77 HPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPawRKRDQKR 156
Cdd:cd00899   103 HYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDTGRYKMIRHIHDK--RNRDNPN 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034643452 157 IAAQKQEQFKVDREGGLNTVKYHVasrtaLSVGGAPcTVLNIMLD 201
Cdd:cd00899   181 RFALLQNSRERDHSDGLNSLKYKV-----LSIELAP-LYTNILVD 219
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 1-201 1.64e-99

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: 287.56  E-value: 1.64e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452   1 MRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSN--STDYIAMHDVDLLPLNEELDYGFPEaGPFHVASPE--L 76
Cdd:cd00899    24 LHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKdgDWDCFIFHDVDLLPENDRNLYGCEE-GPRHLSVPLdkF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452  77 HPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPawRKRDQKR 156
Cdd:cd00899   103 HYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDTGRYKMIRHIHDK--RNRDNPN 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034643452 157 IAAQKQEQFKVDREGGLNTVKYHVasrtaLSVGGAPcTVLNIMLD 201
Cdd:cd00899   181 RFALLQNSRERDHSDGLNSLKYKV-----LSIELAP-LYTNILVD 219
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 67-143 1.10e-31

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: 110.39  E-value: 1.10e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034643452  67 GPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRH 143
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYH 77
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 1-201 1.64e-99

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: 287.56  E-value: 1.64e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452   1 MRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSN--STDYIAMHDVDLLPLNEELDYGFPEaGPFHVASPE--L 76
Cdd:cd00899    24 LHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKdgDWDCFIFHDVDLLPENDRNLYGCEE-GPRHLSVPLdkF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643452  77 HPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPawRKRDQKR 156
Cdd:cd00899   103 HYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDTGRYKMIRHIHDK--RNRDNPN 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034643452 157 IAAQKQEQFKVDREGGLNTVKYHVasrtaLSVGGAPcTVLNIMLD 201
Cdd:cd00899   181 RFALLQNSRERDHSDGLNSLKYKV-----LSIELAP-LYTNILVD 219
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 67-143 1.10e-31

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: 110.39  E-value: 1.10e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034643452  67 GPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRH 143
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYH 77
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 4-56 4.15e-13

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: 63.63  E-value: 4.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034643452   4 FLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSNSTDY--IAMHDVDLLPLN 56
Cdd:pfam13733  64 FLQRQQLDYGIYVIEQAGNGTFNRAKLLNVGFLEALKDYDYdcFIFHDVDLIPED 118
 
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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