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Conserved domains on  [gi|13929462|ref|NP_001488|]
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beta-1,4-galactosyltransferase 1 isoform 1 [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

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 ...
 175-393 2.18e-145

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: 411.20  E-value: 2.18e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 175 PHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPM 254
Cdd:cd00899   1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 255 NDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAV 334
Cdd:cd00899  81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13929462 335 VGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYQVLDVQRYPLYTQITVD 393
Cdd:cd00899 161 TGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 175-393 2.18e-145

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: 411.20  E-value: 2.18e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 175 PHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPM 254
Cdd:cd00899   1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 255 NDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAV 334
Cdd:cd00899  81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13929462 335 VGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYQVLDVQRYPLYTQITVD 393
Cdd:cd00899 161 TGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 138-262 8.69e-89

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: 263.94  E-value: 8.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462   138 VGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQA 217
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 13929462   218 GDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRC 262
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 175-393 2.18e-145

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: 411.20  E-value: 2.18e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 175 PHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPM 254
Cdd:cd00899   1 RHKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 255 NDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAV 334
Cdd:cd00899  81 NDRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13929462 335 VGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYQVLDVQRYPLYTQITVD 393
Cdd:cd00899 161 TGRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 138-262 8.69e-89

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: 263.94  E-value: 8.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462   138 VGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQA 217
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVQPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 13929462   218 GDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRC 262
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 267-343 1.42e-36

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: 127.73  E-value: 1.42e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13929462   267 RHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRH 343
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYH 77
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 219-325 7.61e-08

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: 51.81  E-value: 7.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 219 DTIFNRAKLLNVGFQEAlkDYDYtcFVFSDVDLIPMNDhnayrcFSQpRHISVAMDKFGFSLPYV--------QYF-GGV 289
Cdd:cd06420  62 DEGFRKAKIRNKAIAAA--KGDY--LIFIDGDCIPHPD------FIA-DHIELAEPGVFLSGSRVllneklteRGIrGCN 130

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13929462 290 SALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRG 325
Cdd:cd06420 131 MSFWKKDLLAVNGFDEEFTGWGGEDSELVARLLNSG 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 180-330 6.38e-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: 48.66  E-value: 6.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 180 IIIPFRNRQEHLKYWLYYLhpvLQRQQLDYGIYVINQA-----------------------GDTIFNRAKLLNVGFQEAl 236
Cdd:cd00761   1 VIIPAYNEEPYLERCLESL---LAQTYPNFEVIVVDDGstdgtleileeyakkdprvirviNEENQGLAAARNAGLKAA- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462 237 kDYDYtcFVFSDVDLIPMNDH--NAYRCFSQPRHISVAmdkfgfslpyvqYFGGVSALSKQQFLTINGFPNNYWGWggED 314
Cdd:cd00761  77 -RGEY--ILFLDADDLLLPDWleRLVAELLADPEADAV------------GGPGNLLFRRELLEEIGGFDEALLSG--EE 139

                       170
                ....*....|....*.
gi 13929462 315 DDIFNRLVFRGMSISR 330
Cdd:cd00761 140 DDDFLLRLLRGGKVAF 155
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 223-331 6.36e-03

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: 38.03  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929462   223 NRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYF---GGVSALSKQQFLT 299
Cdd:pfam10111  98 KFEKQLKIATSLALQENIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVFYSPLAIFFapnSSNALINRQAFIE 177

                          90       100       110
                  ....*....|....*....|....*....|..
gi 13929462   300 INGFPNNYWGWGGEDDDIFNRLVFRGMSISRP 331
Cdd:pfam10111 178 VGGFDESFRGHGAEDFDIFLRLAARYPFVAVM 209
 
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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