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Conserved domains on  [gi|188528672|ref|NP_062778|]
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beta-1,4-galactosyltransferase 4 [Mus musculus]

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 ...
 122-339 9.29e-129

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: 366.91  E-value: 9.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899    2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 202 DFNLYTCGDQPKHLVVGRNSTGYRLRYSKYFGGVTALSREQFLKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRPKPDV 281
Cdd:cd00899   82 DRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDT 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 188528672 282 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 339
Cdd:cd00899  162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 122-339 9.29e-129

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: 366.91  E-value: 9.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899    2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 202 DFNLYTCGDQPKHLVVGRNSTGYRLRYSKYFGGVTALSREQFLKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRPKPDV 281
Cdd:cd00899   82 DRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDT 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 188528672 282 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 339
Cdd:cd00899  162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 85-208 6.83e-83

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: 246.99  E-value: 6.83e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672   85 RGQSKLVFKPDLTLEEIEAENPKV-SRGRYHPEECKALQRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQT 163
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVqPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 188528672  164 GSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPENDFNLYTC 208
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 112-274 2.64e-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: 42.04  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 112 RYHPEECKALQRVAILIPHRNREKHLIYLLEHLhpflqrQQLDYG-----IYIIHQtGS------------KKFNRAKLL 174
Cdd:COG1215   19 ARRRRAPADLPRVSVIIPAYNEEAVIEETLRSL------LAQDYPkekleVIVVDD-GStdetaeiarelaAEYPRVRVI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 175 ----NVGYLEALkeeNW-------DCFVFHDVDLVPENDF--NLYTCGDQPKHLVVGRNStgyrlryskyfggvtALSRE 241
Cdd:COG1215   92 erpeNGGKAAAL---NAglkaargDIVVFLDADTVLDPDWlrRLVAAFADPGVGASGANL---------------AFRRE 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 188528672 242 QFLKVNGFSNNYWgwgGEDDDLRLRVELHKMKI 274
Cdd:COG1215  154 ALEEVGGFDEDTL---GEDLDLSLRLLRAGYRI 183
 
Name Accession Description Interval E-value
b4GalT cd00899
Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core ...
 122-339 9.29e-129

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: 366.91  E-value: 9.29e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 122 QRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQTGSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPEN 201
Cdd:cd00899    2 HKVAIIVPFRNRFEHLLIFLPHLHPFLQRQQLDYRIFVIEQVGNFRFNRAKLLNVGFLEALKDGDWDCFIFHDVDLLPEN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 202 DFNLYTCGDQPKHLVVGRNSTGYRLRYSKYFGGVTALSREQFLKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRPKPDV 281
Cdd:cd00899   82 DRNLYGCEEGPRHLSVPLDKFHYKLPYKTYFGGVLALTREQFRKVNGFSNAYWGWGGEDDDLYNRIKAAGLKITRPSGDT 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 188528672 282 GKYTMIFHTRDKGNEVNMGRMKLLQQMSRVWKTDGLSSCSYRLLSVEHNPLYANITVD 339
Cdd:cd00899  162 GRYKMIRHIHDKRNRDNPNRFALLQNSRERDHSDGLNSLKYKVLSIELAPLYTNILVD 219
Glyco_transf_7N pfam13733
N-terminal region of glycosyl transferase group 7; This is the N-terminal half of a family of ...
 85-208 6.83e-83

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: 246.99  E-value: 6.83e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672   85 RGQSKLVFKPDLTLEEIEAENPKV-SRGRYHPEECKALQRVAILIPHRNREKHLIYLLEHLHPFLQRQQLDYGIYIIHQT 163
Cdd:pfam13733   1 VGPLKVNFNSPPTLEEVEKKNPLVqPGGRYKPPDCKARHKVAIIIPYRNREEHLRYLLYHLHPFLQRQQLDYGIYVIEQA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 188528672  164 GSKKFNRAKLLNVGYLEALKEENWDCFVFHDVDLVPENDFNLYTC 208
Cdd:pfam13733  81 GNGTFNRAKLLNVGFLEALKDYDYDCFIFHDVDLIPEDDRNLYTC 125
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 213-289 1.18e-35

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: 124.26  E-value: 1.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188528672  213 KHLVVGRNSTGYRLRYSKYFGGVTALSREQFLKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRPKPDVGKYTMIFH 289
Cdd:pfam02709   1 RHLSVALDKFGYKLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGDIGRYYMLYH 77
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 168-289 3.15e-07

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: 49.88  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 168 FNRAKLLNvgylEALKEENWDCFVFHDVDLVPENDF-----NLYtcgdQPKHLVVGRnstgyRLRYSKYF------GGVT 236
Cdd:cd06420   65 FRKAKIRN----KAIAAAKGDYLIFIDGDCIPHPDFiadhiELA----EPGVFLSGS-----RVLLNEKLtergirGCNM 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188528672 237 ALSREQFLKVNGFSNNYWGWGGEDDDLRLRVELHKMKISRpkpdVGKYTMIFH 289
Cdd:cd06420  132 SFWKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIKFRK----LKFAAIVFH 180
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 126-274 1.90e-05

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: 44.03  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 126 ILIPHRNREKHLIYLLEHL----HPFLQ----------------RQQLDYGIYIIHQTGSKKFNRAKLLNVGyLEALKEe 185
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLlaqtYPNFEvivvddgstdgtleilEEYAKKDPRVIRVINEENQGLAAARNAG-LKAARG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 186 nwDCFVFHDVDLVPENDF--NLYTCGDQPKHLVVGrnstgyrlryskYFGGVTALSREQFLKVNGFSNNYWGWGGEDDDL 263
Cdd:cd00761   79 --EYILFLDADDLLLPDWleRLVAELLADPEADAV------------GGPGNLLFRRELLEEIGGFDEALLSGEEDDDFL 144

                        170
                 ....*....|.
gi 188528672 264 RLRVELHKMKI 274
Cdd:cd00761  145 LRLLRGGKVAF 155
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 112-274 2.64e-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: 42.04  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 112 RYHPEECKALQRVAILIPHRNREKHLIYLLEHLhpflqrQQLDYG-----IYIIHQtGS------------KKFNRAKLL 174
Cdd:COG1215   19 ARRRRAPADLPRVSVIIPAYNEEAVIEETLRSL------LAQDYPkekleVIVVDD-GStdetaeiarelaAEYPRVRVI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528672 175 ----NVGYLEALkeeNW-------DCFVFHDVDLVPENDF--NLYTCGDQPKHLVVGRNStgyrlryskyfggvtALSRE 241
Cdd:COG1215   92 erpeNGGKAAAL---NAglkaargDIVVFLDADTVLDPDWlrRLVAAFADPGVGASGANL---------------AFRRE 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 188528672 242 QFLKVNGFSNNYWgwgGEDDDLRLRVELHKMKI 274
Cdd:COG1215  154 ALEEVGGFDEDTL---GEDLDLSLRLLRAGYRI 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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