GGTA1_BOVIN
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 03-AUG-2022, entry version 167.
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}.
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DR EMBL; J04989; AAA30558.1; -; mRNA.
DR PIR; A44785; A44785.
DR RefSeq; NP_803477.1; NM_177511.2.
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.ENSBTAP00000016033; -.
DR BindingDB; P14769; -.
DR ChEMBL; CHEMBL2069158; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR PaxDb; P14769; -.
DR PRIDE; P14769; -.
DR Ensembl; ENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
DR Ensembl; ENSBTAT00000084155; ENSBTAP00000074297; ENSBTAG00000012090.
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 OrthoDB; 1204439at2759; -.
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; 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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 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
