KEGG   ENZYME: 2.4.1.122Help
Entry
EC 2.4.1.122                Enzyme                                 

Name
N-acetylgalactosaminide beta-1,3-galactosyltransferase;
glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase;
uridine diphosphogalactose-mucin beta-(1->3)-galactosyltransferase;
UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D-galactosyltransferase;
UDP-Gal:alpha-D-GalNAc-1,3-alpha-D-GalNAc-diphosphoundecaprenol beta-1,3-galactosyltransferase;
wbnJ (gene name);
wbiP (gene name);
C1GALT1 (gene name);
UDP-alpha-D-galactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D-galactosyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-alpha-D-galactose:N-acetyl-alpha-D-galactosaminyl-R beta-1,3-galactosyltransferase (configuration-inverting)
Reaction(IUBMB)
UDP-alpha-D-galactose + N-acetyl-alpha-D-galactosaminyl-R = UDP + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R [RN:R05908]
Reaction(KEGG)
R05908(G);
(other) R10436
Show
Substrate
UDP-alpha-D-galactose [CPD:C00052];
N-acetyl-alpha-D-galactosaminyl-R [CPD:C04387]
Product
UDP [CPD:C00015];
beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R [CPD:C04750]
Comment
The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
History
EC 2.4.1.122 created 1984 (EC 2.4.1.307 created 2013, incorporated 2016), modified 2016
Pathway
Mucin type O-glycan biosynthesis
Metabolic pathways
Orthology
K00731  
glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
K21366  
N-acetylgalactosaminide beta-1,3-galactosyltransferase
Genes
HSA: 
56913(C1GALT1)
PTR: 
472288(C1GALT1)
PPS: 
100977740(C1GALT1)
GGO: 
101145951(C1GALT1)
PON: 
100452461(C1GALT1)
NLE: 
100583301(C1GALT1)
MCC: 
696870(C1GALT1)
MCF: 
102137839(C1GALT1)
CSAB: 
103226504(C1GALT1)
RRO: 
104668754(C1GALT1)
CJC: 
100406487(C1GALT1)
SBQ: 
101029936(C1GALT1)
MMU: 
94192(C1galt1)
RNO: 
65044(C1galt1)
CGE: 
100761169(C1galt1)
NGI: 
103751705(C1galt1)
HGL: 
101704643(C1galt1)
OCU: 
100359047(C1GALT1)
TUP: 
102479007(C1GALT1)
CFA: 
482314(C1GALT1)
AML: 
100483848(C1GALT1)
UMR: 
103658758(C1GALT1)
FCA: 
101096459(C1GALT1)
PTG: 
102965358(C1GALT1)
AJU: 
106970015(C1GALT1)
BTA: 
539417(C1GALT1)
BOM: 
102287025(C1GALT1)
PHD: 
CHX: 
102169248(C1GALT1)
OAS: 
SSC: 
100525767(C1GALT1)
CFR: 
102514986(C1GALT1)
BACU: 
103001219(C1GALT1)
LVE: 
103071088(C1GALT1)
ECB: 
100063865(C1GALT1)
MYB: 
MYD: 
102754234(C1GALT1)
HAI: 
109394810(C1GALT1)
PALE: 
102883390(C1GALT1)
LAV: 
100670784(C1GALT1)
SHR: 
100932643(C1GALT1)
OAA: 
GGA: 
420575(C1GALT1)
MGP: 
100542429(C1GALT1)
CJO: 
107309116(C1GALT1)
APLA: 
101797632(C1GALT1)
TGU: 
100221974(C1GALT1)
GFR: 
102032158(C1GALT1)
FAB: 
101810221(C1GALT1)
PHI: 
CCW: 
104689153(C1GALT1)
FPG: 
101923797(C1GALT1)
FCH: 
102059381(C1GALT1)
CLV: 
102088254(C1GALT1)
AAM: 
ASN: 
AMJ: 
PSS: 
102460792(C1GALT1)
CMY: 
CPIC: 
ACS: 
PBI: 
GJA: 
XLA: 
XTR: 
DRE: 
337131(c1galt1b) 555344(si:dkey-202e17.1) 557675(c1galt1a)
IPU: 
TRU: 
TNG: 
LCO: 
MZE: 
OLA: 
XMA: 
SASA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD10181(Dsim_GD10181) Dsimw501_GD12540(Dsim_GD12540) Dsimw501_GD12541(Dsim_GD12541) Dsimw501_GD13582(Dsim_GD13582) Dsimw501_GD22375(Dsim_GD22375) Dsimw501_GD22798(Dsim_GD22798) Dsimw501_GD23186(Dsim_GD23186) Dsimw501_GD23187(Dsim_GD23187) Dsimw501_GD24465(Dsim_GD24465) Dsimw501_GD27301(Dsim_GD27301)
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
BIM: 
BTER: 
SOC: 
AEC: 
HST: 
CFO: 
NVI: 
TCA: 
BMOR: 
DPL: 
PXY: 
API: 
PHU: 
DPX: 
ISC: 
CEL: 
CELE_C38H2.2(C38H2.2)
CBR: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
SMM: 
NVE: 
ADF: 
HMG: 
OTA: 
MBR: 
SRE: 
FCY: 
TPS: 
AAF: 
NGD: 
NGA_0449900(C1GALT1)
PIF: 
PSOJ: 
SPAR: 
EHX: 
ECG: 
EAL: 
SEEC: 
PLU: 
plu4819(wblT)
 » show all
Taxonomy
Reference
1  [PMID:6789880]
  Authors
Hesford FJ, Berger EG, Van den Eijnden DH.
  Title
Identification of the product formed by human erythrocyte galactosyltransferase.
  Journal
Biochim. Biophys. Acta. 659 (1981) 302-11.
Reference
2  [PMID:6801057]
  Authors
Mendicino J, Sivakami S, Davila M, Chandrasekaran EV.
  Title
Purification and properties of UDP-gal:N-acetylgalactosaminide mucin: beta 1,3-galactosyltransferase from swine trachea mucosa.
  Journal
J. Biol. Chem. 257 (1982) 3987-94.
Reference
3  [PMID:6366476]
  Authors
Schachter H, Narasimhan S, Gleeson P, Vella G.
  Title
Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type.
  Journal
Methods. Enzymol. 98 (1983) 98-134.
Reference
4  [PMID:11677243]
  Authors
Ju T, Brewer K, D'Souza A, Cummings RD, Canfield WM
  Title
Cloning and expression of human core 1 beta1,3-galactosyltransferase.
  Journal
J. Biol. Chem. 277 (2002) 178-86.
  Sequence
[hsa:56913] [mmu:94192] [rno:65044] [cel:CELE_C38H2.2] [dme:Dmel_CG9520 Dmel_CG8708]
Reference
5  [PMID:18179256]
  Authors
Yi W, Perali RS, Eguchi H, Motari E, Woodward R, Wang PG
  Title
Characterization of a bacterial beta-1,3-galactosyltransferase with application in the synthesis of tumor-associated T-antigen mimics.
  Journal
Biochemistry. 47 (2008) 1241-8.
Reference
6  [PMID:20418877]
  Authors
Woodward R, Yi W, Li L, Zhao G, Eguchi H, Sridhar PR, Guo H, Song JK, Motari E, Cai L, Kelleher P, Liu X, Han W, Zhang W, Ding Y, Li M, Wang PG
  Title
In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz.
  Journal
Nat. Chem. Biol. 6 (2010) 418-23.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
97089-61-7

DBGET integrated database retrieval system