ID GGTA1_BOVIN Reviewed; 368 AA. AC P14769; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=N-acetyllactosaminide alpha-1,3-galactosyltransferase; DE EC=2.4.1.87 {ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052}; DE AltName: Full=UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase; DE Short=Galactosyltransferase; GN Name=GGTA1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2503516; DOI=10.1016/s0021-9258(18)71676-1; RA Joziasse D.H., Shaper J.H., van den Eijnden D.H., van Tunen A.J., RA Shaper N.L.; RT "Bovine alpha 1-->3-galactosyltransferase: isolation and characterization RT of a cDNA clone. Identification of homologous sequences in human genomic RT DNA."; RL J. Biol. Chem. 264:14290-14297(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-368 IN COMPLEX WITH MANGANESE RP AND SUBSTRATE ANALOGS, METAL-BINDING, AND ACTIVE SITE. RX PubMed=11179209; DOI=10.1093/emboj/20.4.638; RA Gastinel L.N., Bignon C., Misra A.K., Hindsgaul O., Shaper J.H., RA Joziasse D.H.; RT "Bovine alpha1,3-galactosyltransferase catalytic domain structure and its RT relationship with ABO histo-blood group and glycosphingolipid RT glycosyltransferases."; RL EMBO J. 20:638-649(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 80-368 IN COMPLEX WITH MANGANESE RP AND UDP, MUTAGENESIS OF ARG-365, METAL-BINDING, AND CATALYTIC ACTIVITY. RX PubMed=11592969; DOI=10.1074/jbc.m108828200; RA Boix E., Swaminathan G.J., Zhang Y., Natesh R., Brew K., Acharya K.R.; RT "Structure of UDP complex of UDP-galactose:beta-galactoside-alpha-1,3- RT galactosyltransferase at 1.53-A resolution reveals a conformational change RT in the catalytically important C-terminus."; RL J. Biol. Chem. 276:48608-48614(2001). RN [4] {ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4} RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 80-368 IN COMPLEX WITH MANGANESE; RP UDP AND SUBSTRATE ANALOGS, METAL-BINDING, AND CATALYTIC ACTIVITY. RX PubMed=12011052; DOI=10.1074/jbc.m202631200; RA Boix E., Zhang Y., Swaminathan G.J., Brew K., Acharya K.R.; RT "Structural basis of ordered binding of donor and acceptor substrates to RT the retaining glycosyltransferase, alpha-1,3-galactosyltransferase."; RL J. Biol. Chem. 277:28310-28318(2002). CC -!- FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by CC catalyzing the transfer of a galactose residue, with an alpha-1,3 CC linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide CC borne by a glycoprotein or a glycolipid. Preferentially glycosylates CC proteins, can synthesize galactose-alpha(1,3)-galactose on CC glycoproteins but cannot synthesize the glycolipid called CC isoglobotrihexosylceramide or isogloboside 3 (iGb3). CC {ECO:0000250|UniProtKB:P23336}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl CC derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)- CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + CC H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507, CC ChEBI:CHEBI:138024; EC=2.4.1.87; CC Evidence={ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, CC ECO:0000269|PubMed:12011052}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:11179209, CC ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052}; CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single- CC pass type II membrane protein. Note=Membrane-bound form in trans CC cisternae of Golgi. CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The CC manganese ion interacts with the beta-phosphate group of UDP and may CC also have a role in catalysis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04989; AAA30558.1; -; mRNA. DR PIR; A44785; A44785. DR RefSeq; NP_803477.1; NM_177511.2. DR RefSeq; XP_005212979.1; XM_005212922.3. DR RefSeq; XP_005212980.1; XM_005212923.3. DR RefSeq; XP_005212981.1; XM_005212924.3. DR PDB; 1FG5; X-ray; 2.80 A; N=80-368. DR PDB; 1G8O; X-ray; 2.30 A; A=80-368. DR PDB; 1G93; X-ray; 2.50 A; A=80-368. DR PDB; 1GWV; X-ray; 2.50 A; A/B=80-368. DR PDB; 1GWW; X-ray; 1.80 A; A/B=80-368. DR PDB; 1GX0; X-ray; 1.80 A; A/B=80-368. DR PDB; 1GX4; X-ray; 1.46 A; A/B=80-368. DR PDB; 1K4V; X-ray; 1.53 A; A/B=80-368. DR PDB; 1O7O; X-ray; 1.97 A; A/B=80-368. DR PDB; 1O7Q; X-ray; 1.30 A; A/B=80-368. DR PDB; 1VZT; X-ray; 2.00 A; A/B=80-368. DR PDB; 1VZU; X-ray; 1.97 A; A/B=80-368. DR PDB; 1VZX; X-ray; 1.97 A; A/B=80-368. DR PDB; 2JCJ; X-ray; 2.01 A; A=80-365. DR PDB; 2JCK; X-ray; 1.80 A; A=80-368. DR PDB; 2JCL; X-ray; 3.29 A; A/B=80-368. DR PDB; 2JCO; X-ray; 2.57 A; A=80-368. DR PDB; 2VFZ; X-ray; 2.40 A; A/B=80-368. DR PDB; 2VS3; X-ray; 2.20 A; A/B=80-368. DR PDB; 2VS4; X-ray; 1.77 A; A/B=80-368. DR PDB; 2VS5; X-ray; 1.82 A; A/B=80-365. DR PDB; 2VXL; X-ray; 2.70 A; A=82-358. DR PDB; 2VXM; X-ray; 2.82 A; A/B/C/D=82-354. DR PDB; 2WGZ; X-ray; 2.12 A; A/B=80-368. DR PDB; 5NR9; X-ray; 1.70 A; A/B=80-368. DR PDB; 5NRB; X-ray; 2.24 A; A/B=80-368. DR PDB; 5NRD; X-ray; 2.12 A; A/B=80-368. DR PDB; 5NRE; X-ray; 1.98 A; A/B=80-368. DR PDBsum; 1FG5; -. DR PDBsum; 1G8O; -. DR PDBsum; 1G93; -. DR PDBsum; 1GWV; -. DR PDBsum; 1GWW; -. DR PDBsum; 1GX0; -. DR PDBsum; 1GX4; -. DR PDBsum; 1K4V; -. DR PDBsum; 1O7O; -. DR PDBsum; 1O7Q; -. DR PDBsum; 1VZT; -. DR PDBsum; 1VZU; -. DR PDBsum; 1VZX; -. DR PDBsum; 2JCJ; -. DR PDBsum; 2JCK; -. DR PDBsum; 2JCL; -. DR PDBsum; 2JCO; -. DR PDBsum; 2VFZ; -. DR PDBsum; 2VS3; -. DR PDBsum; 2VS4; -. DR PDBsum; 2VS5; -. DR PDBsum; 2VXL; -. DR PDBsum; 2VXM; -. DR PDBsum; 2WGZ; -. DR PDBsum; 5NR9; -. DR PDBsum; 5NRB; -. DR PDBsum; 5NRD; -. DR PDBsum; 5NRE; -. DR AlphaFoldDB; P14769; -. DR SMR; P14769; -. DR STRING; 9913.ENSBTAP00000065603; -. DR BindingDB; P14769; -. DR ChEMBL; CHEMBL2069158; -. DR CAZy; GT6; Glycosyltransferase Family 6. DR GlyCosmos; P14769; 1 site, No reported glycans. DR PaxDb; 9913-ENSBTAP00000016033; -. DR Ensembl; ENSBTAT00000016033.3; ENSBTAP00000016033.2; ENSBTAG00000012090.5. DR Ensembl; ENSBTAT00000084155.1; ENSBTAP00000074297.1; ENSBTAG00000012090.5. DR GeneID; 281780; -. DR KEGG; bta:281780; -. DR CTD; 2681; -. DR VEuPathDB; HostDB:ENSBTAG00000012090; -. DR eggNOG; ENOG502QW2H; Eukaryota. DR GeneTree; ENSGT00950000182858; -. DR HOGENOM; CLU_062445_1_0_1; -. DR InParanoid; P14769; -. DR OMA; ELAWHLH; -. DR TreeFam; TF330991; -. DR BRENDA; 2.4.1.87; 908. DR UniPathway; UPA00378; -. DR EvolutionaryTrace; P14769; -. DR PRO; PR:P14769; -. DR Proteomes; UP000009136; Chromosome 11. DR Bgee; ENSBTAG00000012090; Expressed in thymus and 107 other cell types or tissues. DR ExpressionAtlas; P14769; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031982; C:vesicle; IBA:GO_Central. DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047276; F:N-acetyllactosaminide 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR CDD; cd02515; Glyco_transf_6; 1. DR InterPro; IPR005076; Glyco_trans_6. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR10462; GLYCOSYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR10462:SF26; N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYLTRANSFERASE; 1. DR Pfam; PF03414; Glyco_transf_6; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..368 FT /note="N-acetyllactosaminide alpha-1,3- FT galactosyltransferase" FT /id="PRO_0000157298" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..22 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 23..368 FT /note="Lumenal" FT /evidence="ECO:0000255" FT ACT_SITE 317 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:11179209, FT ECO:0007744|PDB:1G8O" FT BINDING 134..139 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11179209, FT ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, FT ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, FT ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, FT ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, FT ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, FT ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, FT ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, FT ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, FT ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ" FT BINDING 225..227 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11179209, FT ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, FT ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, FT ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, FT ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, FT ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, FT ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, FT ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, FT ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, FT ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ" FT BINDING 225 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:11179209, FT ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, FT ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, FT ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, FT ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, FT ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, FT ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, FT ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, FT ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, FT ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, FT ECO:0007744|PDB:2WGZ" FT BINDING 227 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:11179209, FT ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, FT ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, FT ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, FT ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, FT ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, FT ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, FT ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, FT ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, FT ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, FT ECO:0007744|PDB:2WGZ" FT BINDING 247..250 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, FT ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, FT ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, FT ECO:0007744|PDB:2WGZ" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12011052, FT ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, FT ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, FT ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, FT ECO:0007744|PDB:2WGZ" FT BINDING 359..365 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11592969, FT ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, FT ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, FT ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, FT ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, FT ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, FT ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, FT ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, FT ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, FT ECO:0007744|PDB:2WGZ" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 365 FT /note="R->K: Strongly reduces catalytic efficiency." FT /evidence="ECO:0000269|PubMed:11592969" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:1G93" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:1O7Q" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:1GWW" FT HELIX 115..125 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 139..154 FT /evidence="ECO:0007829|PDB:1O7Q" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:2JCK" FT STRAND 161..168 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 195..212 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 214..217 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 240..246 FT /evidence="ECO:0007829|PDB:1O7Q" FT TURN 248..252 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 279..286 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 288..307 FT /evidence="ECO:0007829|PDB:1O7Q" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 316..326 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:1O7Q" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:2VXM" FT STRAND 353..356 FT /evidence="ECO:0007829|PDB:1O7Q" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:1O7Q" SQ SEQUENCE 368 AA; 43247 MW; 5BC50D6737BDDC33 CRC64; MNVKGKVILS MLVVSTVIVV FWEYIHSPEG SLFWINPSRN PEVGGSSIQK GWWLPRWFNN GYHEEDGDIN EEKEQRNEDE SKLKLSDWFN PFKRPEVVTM TKWKAPVVWE GTYNRAVLDN YYAKQKITVG LTVFAVGRYI EHYLEEFLTS ANKHFMVGHP VIFYIMVDDV SRMPLIELGP LRSFKVFKIK PEKRWQDISM MRMKTIGEHI VAHIQHEVDF LFCMDVDQVF QDKFGVETLG ESVAQLQAWW YKADPNDFTY ERRKESAAYI PFGEGDFYYH AAIFGGTPTQ VLNITQECFK GILKDKKNDI EAQWHDESHL NKYFLLNKPT KILSPEYCWD YHIGLPADIK LVKMSWQTKE YNVVRNNV //