KEGG   ENZYME: 2.4.1.214
Entry
EC 2.4.1.214                Enzyme                                 

Name
glycoprotein 3-alpha-L-fucosyltransferase;
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase;
GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase;
GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fucalpha1->6GlcNAc)-Asn-peptide) alpha1->3-fucosyltransferase;
GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase;
GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase;
GDP-beta-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
GDP-beta-L-fucose:N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] 3-alpha-L-fucosyltransferase (configuration-retaining)
Reaction(IUBMB)
GDP-beta-L-fucose + N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc}-L-asparaginyl-[protein] [RN:R06015]
Reaction(KEGG)
R06015(G) > R09318(G);
(other) R11318(G)
Substrate
GDP-beta-L-fucose [CPD:C00325];
N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein]
Product
GDP [CPD:C00035];
N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc}-L-asparaginyl-[protein]
Comment
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
History
EC 2.4.1.214 created 2001
Pathway
ec00513  Various types of N-glycan biosynthesis
ec01100  Metabolic pathways
Orthology
K00753  glycoprotein 3-alpha-L-fucosyltransferase
Genes
ZVI: 118078576
BFO: 118405950 118406257 118411908 118412045 118412254 118412440 118413693 118422612 118425677 118426531 118426592 118426593 118429660 118430705 118432514 118432653
BBEL: 109461731 109466362 109467558 109467559 109468794 109470793 109472650 109473253 109474715
SCLV: 120325783 120325811 120326252 120326253 120326461 120327132 120330128 120332423 120335441 120335442 120336318 120343945
SPU: 100890299 100892875 105437757 105440751 105443584 105445519 115921346 115922540 115922761 115925446 115925447 115925451 115925452 115926808 115929731 574917 575118 579774 582389 588755 753114
APLC: 110976930 110977799 110978133 110978134 110980446 110981755 110989209 110989340 110990202 110990203
DME: Dmel_CG6869(FucTA)
DER: 6544519
DSE: 6605753
DSI: Dsimw501_GD14528(Dsim_GD14528)
DAN: 6506328
DSR: 110176209
DWI: 6645794
DGR: 6557543
DAZ: 108613431
DNV: 108651431
DHE: 111595062
DVI: 6622988
MDE: 101901412
LCQ: 111685167
ACOZ: 120953373
AARA: 120896316
AAG: 5575371
AALB: 109414185
CPII: 120423217
BIM: 100748078
BBIF: 117204097
BTER: 100642198
CCAL: 108633042
MGEN: 117220654
NMEA: 116427819
CGIG: 122405483
SOC: 105194752
MPHA: 105830600
AEC: 105151786
ACEP: 105627764
PBAR: 105425145
VEM: 105569385
HST: 105182309
DQU: 106741312
CFO: 105253014
FEX: 115244899
LHU: 105673879
PGC: 109853983
OBO: 105281195
PCF: 106789776
NVI: 100116394
CSOL: 105360968
MDL: 103572507
CCIN: 107265253
APLN: 108745025
OTU: 111424370
BMOR: 101742412
BMAN: 114243659
MSEX: 115447326
BANY: 112054928
PMAC: 106715499
PPOT: 106104327
PXU: 106116844
PRAP: 110992454
ZCE: 119829157
HAW: 110377270
TNL: 113499332
PXY: 105397575
BTAB: 109033726
CLEC: 106668184
HHAL: 106685390
VDE: 111246813
VJA: 111263712
DPTE: 113791393
CEL: CELE_K12H6.3(fut-4)
ATH: AT1G49710(FUT12) AT3G19280(FUT11)
CPAP: 110813783
CIT: 102617014
PVY: 116140879
TCC: 18607941
EGR: 104418734
VRA: 106768760
VAR: 108343376
VUN: 114178538
CCAJ: 109793169
APRC: 113858078
CAM: 101502044
LJA: Lj4g3v0598850.1(Lj4g3v0598850.1)
ADU: 107469717
AIP: 107623116
FVE: 101293079
RCN: 112172265
PPER: 18766662
PMUM: 103335356
PAVI: 110771695
PXB: 103937988
ZJU: 107427081
MNT: 21410140
RCU: 8275299
JCU: 105629829
POP: 7457535
PEU: 105108067
PALZ: 118059215
JRE: 108988882
QSU: 112025720
QLO: 115968668
VVI: 100255469
VRI: 117911323
EGT: 105957556
CSIN: 114277040
BVG: 104904482
SOE: 110778319
NCOL: 116262080
OSA: 4345809
DOSA: Os08t0472600-01(Os08g0472600)
OBR: 102709390
BDI: 100834636
ATS: 109765104
SBI: 8056895
SITA: 101766834
PHAI: 112897037
PEQ: 110029537
AOF: 109849943
ATR: 18421358
SMO: SELMODRAFT_452935(FucTA)
PPP: 112288886
SMIN: v1.2.020659.t1(symbB.v1.2.020659.t1)
 » show all
Reference
1  [PMID:11420147]
  Authors
Wilson IB, Rendic D, Freilinger A, Dumic J, Altmann F, Mucha J, Muller S, Hauser MT.
  Title
Cloning and expression of cDNAs encoding alpha1,3-fucosyltransferase homologues from Arabidopsis thaliana.
  Journal
Biochim Biophys Acta 1527:88-96 (2001)
DOI:10.1016/S0304-4165(01)00151-9
  Sequence
[ath:AT3G19280]
Reference
2  [PMID:11382750]
  Authors
Fabini G, Freilinger A, Altmann F, Wilson IB
  Title
Identification of core alpha 1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseadish peroxidase epitope.
  Journal
J Biol Chem 276:28058-67 (2001)
DOI:10.1074/jbc.M100573200
  Sequence
Reference
3  [PMID:10419500]
  Authors
Leiter H, Mucha J, Staudacher E, Grimm R, Glossl J, Altmann F.
  Title
Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase from mung beans.
  Journal
J Biol Chem 274:21830-9 (1999)
DOI:10.1074/jbc.274.31.21830
  Sequence
[vra:106768760]
Reference
4  [PMID:10567717]
  Authors
van Tetering A, Schiphorst WE, van den Eijnden DH, van Die I.
  Title
Characterization of a core alpha1-->3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex-type N-glycans.
  Journal
FEBS Lett 461:311-4 (1999)
DOI:10.1016/S0014-5793(99)01489-1
Reference
5  [PMID:1868856]
  Authors
Staudacher E, Altmann F, Glossl J, Marz L, Schachter H, Kamerling JP, Hard K, Vliegenthart JF.
  Title
GDP-fucose: beta-N-acetylglucosamine (Fuc to (Fuc alpha 1----6GlcNAc)-Asn-peptide)alpha 1----3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine.
  Journal
Eur J Biochem 199:745-51 (1991)
DOI:10.1111/j.1432-1033.1991.tb16179.x
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.214
IUBMB Enzyme Nomenclature: 2.4.1.214
ExPASy - ENZYME nomenclature database: 2.4.1.214
BRENDA, the Enzyme Database: 2.4.1.214
CAS: 68247-53-0

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