KEGG   ENZYME: 2.4.1.132Help
Entry
EC 2.4.1.132                Enzyme                                 

Name
GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase;
Alg2 mannosyltransferase (ambiguous);
ALG2 (gene name, ambiguous);
glycolipid 3-alpha-mannosyltransferase;
GDP-mannose:glycolipid 3-alpha-D-mannosyltransferase;
GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
GDP-D-mannose:D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 3-alpha-mannosyltransferase
Reaction(IUBMB)
GDP-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol [RN:R05002 R05973]
Reaction(KEGG)
Substrate
GDP-D-mannose [CPD:C00096];
D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Product
GDP [CPD:C00035];
D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Comment
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
History
EC 2.4.1.132 created 1984, modified 2011, modified 2012
Pathway
N-Glycan biosynthesis
Various types of N-glycan biosynthesis
Metabolic pathways
Orthology
K03843  
alpha-1,3/alpha-1,6-mannosyltransferase
Genes
HSA: 
85365(ALG2)
PTR: 
472993(ALG2)
PPS: 
100984805(ALG2)
GGO: 
101128869(ALG2)
PON: 
100451740(ALG2)
MCC: 
714850(ALG2)
MCF: 
102146841(ALG2)
MMU: 
56737(Alg2)
RNO: 
313231(Alg2)
CGE: 
100768412(Alg2)
HGL: 
101717738(Alg2)
TUP: 
CFA: 
474780(ALG2)
AML: 
FCA: 
101084066(ALG2)
PTG: 
102963679(ALG2)
BTA: 
538899(ALG2)
BOM: 
102282554(ALG2)
PHD: 
102324420(ALG2)
CHX: 
102172999(ALG2)
SSC: 
100113423(ALG2)
CFR: 
102523932(ALG2)
BACU: 
102999901(ALG2)
LVE: 
103071670(ALG2)
ECB: 
100054840(ALG2)
MYB: 
102241662(ALG2)
MYD: 
102764897(ALG2)
PALE: 
102880508(ALG2)
MDO: 
100011371(ALG2)
SHR: 
100913580(ALG2)
OAA: 
100092424(ALG2)
GGA: 
420998(ALG2)
MGP: 
TGU: 
FAB: 
101820728(ALG2)
PHI: 
102103653(ALG2)
APLA: 
101795871(ALG2)
FPG: 
101912340(ALG2)
FCH: 
102058016(ALG2)
CLV: 
102093093(ALG2)
ASN: 
102370298(ALG2)
AMJ: 
102564853(ALG2)
PSS: 
102460786(ALG2)
CMY: 
PBI: 
103051382(ALG2)
XLA: 
446622(alg2)
XTR: 
DRE: 
403068(alg2)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102353262(ALG2)
CMK: 
103181173(alg2)
BFO: 
CIN: 
SPU: 
589943(alg2)
DME: 
DPO: 
DAN: 
DER: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
AME: 
551972(GB17208)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_F09E5.2(F09E5.2)
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0589600-01(Os04g0589600)
OBR: 
BDI: 
SBI: 
SORBI_06g026860(SORBIDRAFT_06g026860)
ZMA: 
100279297(csu425(gct))
SITA: 
ATR: 
s00044p00168360(AMTR_s00044p00168360)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
MIS: 
MPP: 
BPG: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YGL065C(ALG2)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0D04140(NCAS0D04140)
NDI: 
NDAI_0I00780(NDAI0I00780)
TPF: 
TPHA_0J02410(TPHA0J02410)
TBL: 
TBLA_0B05350(TBLA0B05350)
TDL: 
TDEL_0E05270(TDEL0E05270)
KAF: 
KAFR_0K02320(KAFR0K02320)
DHA: 
PIC: 
PGU: 
LEL: 
SPAA: 
CAL: 
CTP: 
CDU: 
COT: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_814094(AO090120000461)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
ZTR: 
PFJ: 
BCOM: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
MGL: 
PGR: 
DDI: 
DPP: 
DFA: 
DFA_05987(alg2)
EHI: 
EHI_001990(90.t00023)
EDI: 
ACAN: 
CPV: 
CHO: 
TGO: 
TET: 
PTI: 
TPS: 
PIF: 
NGD: 
GTT: 
TBR: 
Tb927.4.2230(Tb04.1H19.360)
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
TVA: 
 » show all
Taxonomy
Reference
1  [PMID:19282279]
  Authors
Kampf M, Absmanner B, Schwarz M, Lehle L
  Title
Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis.
  Journal
J. Biol. Chem. 284 (2009) 11900-12.
Reference
2  [PMID:16878994]
  Authors
O'Reilly MK, Zhang G, Imperiali B
  Title
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.
  Journal
Biochemistry. 45 (2006) 9593-603.
  Organism
Saccharomyces cerevisiae
  Sequence
[sce:YGL065C]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
81181-76-2

KEGG   ENZYME: 2.4.1.257Help
Entry
EC 2.4.1.257                Enzyme                                 

Name
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase;
GDP-Man:Man2GlcNAc2-PP-Dol alpha-1,6-mannosyltransferase;
Alg2 mannosyltransferase (ambiguous);
ALG2 (gene name, ambiguous);
GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous)
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
GDP-D-mannose:D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-6-mannosyltransferase
Reaction(IUBMB)
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol [RN:R06238]
Reaction(KEGG)
R06238(G)
Show
Substrate
GDP-D-mannose [CPD:C00096];
D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Product
GDP [CPD:C00035];
D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Comment
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation (cf. EC 2.4.1.132) of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
History
EC 2.4.1.257 created 2011, modified 2012
Pathway
N-Glycan biosynthesis
Various types of N-glycan biosynthesis
Metabolic pathways
Orthology
K03843  
alpha-1,3/alpha-1,6-mannosyltransferase
Genes
HSA: 
85365(ALG2)
PTR: 
472993(ALG2)
PPS: 
100984805(ALG2)
GGO: 
101128869(ALG2)
PON: 
100451740(ALG2)
MCC: 
714850(ALG2)
MCF: 
102146841(ALG2)
MMU: 
56737(Alg2)
RNO: 
313231(Alg2)
CGE: 
100768412(Alg2)
HGL: 
101717738(Alg2)
TUP: 
CFA: 
474780(ALG2)
AML: 
FCA: 
101084066(ALG2)
PTG: 
102963679(ALG2)
BTA: 
538899(ALG2)
BOM: 
102282554(ALG2)
PHD: 
102324420(ALG2)
CHX: 
102172999(ALG2)
SSC: 
100113423(ALG2)
CFR: 
102523932(ALG2)
BACU: 
102999901(ALG2)
LVE: 
103071670(ALG2)
ECB: 
100054840(ALG2)
MYB: 
102241662(ALG2)
MYD: 
102764897(ALG2)
PALE: 
102880508(ALG2)
MDO: 
100011371(ALG2)
SHR: 
100913580(ALG2)
OAA: 
100092424(ALG2)
GGA: 
420998(ALG2)
MGP: 
TGU: 
FAB: 
101820728(ALG2)
PHI: 
102103653(ALG2)
APLA: 
101795871(ALG2)
FPG: 
101912340(ALG2)
FCH: 
102058016(ALG2)
CLV: 
102093093(ALG2)
ASN: 
102370298(ALG2)
AMJ: 
102564853(ALG2)
PSS: 
102460786(ALG2)
CMY: 
PBI: 
103051382(ALG2)
XLA: 
446622(alg2)
XTR: 
DRE: 
403068(alg2)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102353262(ALG2)
CMK: 
103181173(alg2)
BFO: 
CIN: 
SPU: 
589943(alg2)
DME: 
DPO: 
DAN: 
DER: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
AME: 
551972(GB17208)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_F09E5.2(F09E5.2)
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0589600-01(Os04g0589600)
OBR: 
BDI: 
SBI: 
SORBI_06g026860(SORBIDRAFT_06g026860)
ZMA: 
100279297(csu425(gct))
SITA: 
ATR: 
s00044p00168360(AMTR_s00044p00168360)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
MIS: 
MPP: 
BPG: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YGL065C(ALG2)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0D04140(NCAS0D04140)
NDI: 
NDAI_0I00780(NDAI0I00780)
TPF: 
TPHA_0J02410(TPHA0J02410)
TBL: 
TBLA_0B05350(TBLA0B05350)
TDL: 
TDEL_0E05270(TDEL0E05270)
KAF: 
KAFR_0K02320(KAFR0K02320)
DHA: 
PIC: 
PGU: 
LEL: 
SPAA: 
CAL: 
CTP: 
CDU: 
COT: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_814094(AO090120000461)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
ZTR: 
PFJ: 
BCOM: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
MGL: 
PGR: 
DDI: 
DPP: 
DFA: 
DFA_05987(alg2)
EHI: 
EHI_001990(90.t00023)
EDI: 
ACAN: 
CPV: 
CHO: 
TGO: 
TET: 
PTI: 
TPS: 
PIF: 
NGD: 
GTT: 
TBR: 
Tb927.4.2230(Tb04.1H19.360)
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
TVA: 
 » show all
Taxonomy
Reference
1  [PMID:19282279]
  Authors
Kampf M, Absmanner B, Schwarz M, Lehle L
  Title
Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis.
  Journal
J. Biol. Chem. 284 (2009) 11900-12.
Reference
2  [PMID:16878994]
  Authors
O'Reilly MK, Zhang G, Imperiali B
  Title
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.
  Journal
Biochemistry. 45 (2006) 9593-603.
  Organism
Saccharomyces cerevisiae
  Sequence
[sce:YGL065C]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system