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Protein

N-acetyllactosaminide alpha-1,3-galactosyltransferase

Gene

GGTA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-galactose on glycoproteins but cannot synthesize the glycolipid called isoglobotrihexosylceramide or isogloboside 3 (iGb3).By similarity

Catalytic activityi

UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.2 Publications

Cofactori

Mn2+3 PublicationsNote: Binds 1 Mn2+ ion per subunit.3 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi225ManganeseCombined sources3 Publications1
Metal bindingi227ManganeseCombined sources3 Publications1
Binding sitei259SubstrateCombined sources1 Publication1
Active sitei317NucleophileCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.87. 908.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyllactosaminide alpha-1,3-galactosyltransferase (EC:2.4.1.872 Publications)
Alternative name(s):
UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase
Short name:
Galactosyltransferase
Gene namesi
Name:GGTA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 22Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST16
Topological domaini23 – 368LumenalSequence analysisAdd BLAST346

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365R → K: Strongly reduces catalytic efficiency. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2069158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001572981 – 368N-acetyllactosaminide alpha-1,3-galactosyltransferaseAdd BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi293N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP14769.
PRIDEiP14769.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012090.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016033.

Chemistry databases

BindingDBiP14769.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi85 – 88Combined sources4
Helixi91 – 93Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi106 – 108Combined sources3
Turni110 – 112Combined sources3
Helixi115 – 125Combined sources11
Beta strandi129 – 135Combined sources7
Helixi139 – 154Combined sources16
Turni156 – 158Combined sources3
Beta strandi161 – 168Combined sources8
Helixi170 – 172Combined sources3
Beta strandi182 – 188Combined sources7
Helixi195 – 212Combined sources18
Helixi214 – 217Combined sources4
Beta strandi219 – 224Combined sources6
Beta strandi226 – 230Combined sources5
Helixi236 – 238Combined sources3
Beta strandi240 – 246Combined sources7
Turni248 – 252Combined sources5
Helixi255 – 257Combined sources3
Beta strandi279 – 286Combined sources8
Helixi288 – 307Combined sources20
Turni313 – 315Combined sources3
Helixi316 – 326Combined sources11
Beta strandi330 – 333Combined sources4
Helixi335 – 337Combined sources3
Helixi341 – 343Combined sources3
Beta strandi347 – 350Combined sources4
Beta strandi353 – 356Combined sources4
Helixi361 – 364Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FG5X-ray2.80N80-368[»]
1G8OX-ray2.30A80-368[»]
1G93X-ray2.50A80-368[»]
1GWVX-ray2.50A/B80-368[»]
1GWWX-ray1.80A/B80-368[»]
1GX0X-ray1.80A/B80-368[»]
1GX4X-ray1.46A/B80-368[»]
1K4VX-ray1.53A/B80-368[»]
1O7OX-ray1.97A/B80-368[»]
1O7QX-ray1.30A/B80-368[»]
1VZTX-ray2.00A/B80-368[»]
1VZUX-ray1.97A/B80-368[»]
1VZXX-ray1.97A/B80-368[»]
2JCJX-ray2.01A80-365[»]
2JCKX-ray1.80A80-368[»]
2JCLX-ray3.29A/B80-368[»]
2JCOX-ray2.57A80-368[»]
2VFZX-ray2.40A/B80-368[»]
2VS3X-ray2.20A/B80-368[»]
2VS4X-ray1.77A/B80-368[»]
2VS5X-ray1.82A/B80-365[»]
2VXLX-ray2.70A82-358[»]
2VXMX-ray2.82A/B/C/D82-354[»]
2WGZX-ray2.12A/B80-368[»]
ProteinModelPortaliP14769.
SMRiP14769.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14769.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 139Substrate bindingCombined sources3 Publications6
Regioni225 – 227Substrate bindingCombined sources3 Publications3
Regioni247 – 250Substrate bindingCombined sources1 Publication4
Regioni359 – 365Substrate bindingCombined sources2 Publications7

Domaini

The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

Sequence similaritiesi

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHE7. Eukaryota.
ENOG4111IPQ. LUCA.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP14769.
KOiK00743.
OMAiAQLQAWW.
OrthoDBiEOG091G0A87.
TreeFamiTF330991.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P14769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVKGKVILS MLVVSTVIVV FWEYIHSPEG SLFWINPSRN PEVGGSSIQK
60 70 80 90 100
GWWLPRWFNN GYHEEDGDIN EEKEQRNEDE SKLKLSDWFN PFKRPEVVTM
110 120 130 140 150
TKWKAPVVWE GTYNRAVLDN YYAKQKITVG LTVFAVGRYI EHYLEEFLTS
160 170 180 190 200
ANKHFMVGHP VIFYIMVDDV SRMPLIELGP LRSFKVFKIK PEKRWQDISM
210 220 230 240 250
MRMKTIGEHI VAHIQHEVDF LFCMDVDQVF QDKFGVETLG ESVAQLQAWW
260 270 280 290 300
YKADPNDFTY ERRKESAAYI PFGEGDFYYH AAIFGGTPTQ VLNITQECFK
310 320 330 340 350
GILKDKKNDI EAQWHDESHL NKYFLLNKPT KILSPEYCWD YHIGLPADIK
360
LVKMSWQTKE YNVVRNNV
Length:368
Mass (Da):43,247
Last modified:April 1, 1990 - v1
Checksum:i5BC50D6737BDDC33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04989 mRNA. Translation: AAA30558.1.
PIRiA44785.
RefSeqiNP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.3.
XP_005212981.1. XM_005212924.3.
UniGeneiBt.53385.

Genome annotation databases

EnsembliENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
GeneIDi281780.
KEGGibta:281780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04989 mRNA. Translation: AAA30558.1.
PIRiA44785.
RefSeqiNP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.3.
XP_005212981.1. XM_005212924.3.
UniGeneiBt.53385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FG5X-ray2.80N80-368[»]
1G8OX-ray2.30A80-368[»]
1G93X-ray2.50A80-368[»]
1GWVX-ray2.50A/B80-368[»]
1GWWX-ray1.80A/B80-368[»]
1GX0X-ray1.80A/B80-368[»]
1GX4X-ray1.46A/B80-368[»]
1K4VX-ray1.53A/B80-368[»]
1O7OX-ray1.97A/B80-368[»]
1O7QX-ray1.30A/B80-368[»]
1VZTX-ray2.00A/B80-368[»]
1VZUX-ray1.97A/B80-368[»]
1VZXX-ray1.97A/B80-368[»]
2JCJX-ray2.01A80-365[»]
2JCKX-ray1.80A80-368[»]
2JCLX-ray3.29A/B80-368[»]
2JCOX-ray2.57A80-368[»]
2VFZX-ray2.40A/B80-368[»]
2VS3X-ray2.20A/B80-368[»]
2VS4X-ray1.77A/B80-368[»]
2VS5X-ray1.82A/B80-365[»]
2VXLX-ray2.70A82-358[»]
2VXMX-ray2.82A/B/C/D82-354[»]
2WGZX-ray2.12A/B80-368[»]
ProteinModelPortaliP14769.
SMRiP14769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016033.

Chemistry databases

BindingDBiP14769.
ChEMBLiCHEMBL2069158.

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Proteomic databases

PaxDbiP14769.
PRIDEiP14769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
GeneIDi281780.
KEGGibta:281780.

Organism-specific databases

CTDi14594.

Phylogenomic databases

eggNOGiENOG410IHE7. Eukaryota.
ENOG4111IPQ. LUCA.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP14769.
KOiK00743.
OMAiAQLQAWW.
OrthoDBiEOG091G0A87.
TreeFamiTF330991.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.87. 908.

Miscellaneous databases

EvolutionaryTraceiP14769.
PROiP14769.

Gene expression databases

BgeeiENSBTAG00000012090.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGGTA1_BOVIN
AccessioniPrimary (citable) accession number: P14769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.