FUCT_HELPX
ID FUCT_HELPX Reviewed; 478 AA.
AC O30511;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase FucT {ECO:0000303|PubMed:9261149};
DE EC=2.4.1.152 {ECO:0000269|PubMed:12676935, ECO:0000269|PubMed:16150700, ECO:0000269|PubMed:16800635, ECO:0000269|PubMed:17251184, ECO:0000269|PubMed:9261149};
DE AltName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase {ECO:0000305};
GN Name=fucT {ECO:0000312|EMBL:AAB81031.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000312|EMBL:AAB81031.1};
RN [1] {ECO:0000312|EMBL:AAB81031.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802
RC {ECO:0000312|EMBL:AAB81031.1};
RX PubMed=9261149; DOI=10.1074/jbc.272.34.21357;
RA Ge Z., Chan N.W.C., Palcic M.M., Taylor D.E.;
RT "Cloning and heterologous expression of an alpha1,3-fucosyltransferase gene
RT from the gastric pathogen Helicobacter pylori.";
RL J. Biol. Chem. 272:21357-21363(1997).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP REGION, AND MUTAGENESIS OF 347-ASP--CYS-353.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802
RC {ECO:0000303|PubMed:12676935};
RX PubMed=12676935; DOI=10.1074/jbc.m301704200;
RA Ma B., Wang G., Palcic M.M., Hazes B., Taylor D.E.;
RT "C-terminal amino acids of Helicobacter pylori alpha1,3/4
RT fucosyltransferases determine type I and type II transfer.";
RL J. Biol. Chem. 278:21893-21900(2003).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF PHE-350 AND
RP PHE-352.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802
RC {ECO:0000303|PubMed:16150700};
RX PubMed=16150700; DOI=10.1074/jbc.m504415200;
RA Ma B., Lau L.H., Palcic M.M., Hazes B., Taylor D.E.;
RT "A single aromatic amino acid at the carboxyl terminus of Helicobacter
RT pylori {alpha}1,3/4 fucosyltransferase determines substrate specificity.";
RL J. Biol. Chem. 280:36848-36856(2005).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, DOMAIN, REGION, REPEAT, AND
RP MUTAGENESIS OF 456-ARG--LEU-478.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802
RC {ECO:0000303|PubMed:16800635};
RX PubMed=16800635; DOI=10.1021/bi0601297;
RA Lin S.W., Yuan T.M., Li J.R., Lin C.H.;
RT "Carboxyl terminus of Helicobacter pylori alpha1,3-fucosyltransferase
RT determines the structure and stability.";
RL Biochemistry 45:8108-8116(2006).
RN [5] {ECO:0007744|PDB:2NZW, ECO:0007744|PDB:2NZX, ECO:0007744|PDB:2NZY}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-363 IN COMPLEX WITH SUBSTRATE,
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-363, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND MUTAGENESIS OF GLU-95; ARG-195; ASN-240; TYR-246;
RP GLU-249; LYS-250 AND 456-ARG--LEU-478.
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802
RC {ECO:0000303|PubMed:17251184};
RX PubMed=17251184; DOI=10.1074/jbc.m610285200;
RA Sun H.Y., Lin S.W., Ko T.P., Pan J.F., Liu C.L., Lin C.N., Wang A.H.,
RA Lin C.H.;
RT "Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis
RT for lipopolysaccharide variation and inhibitor design.";
RL J. Biol. Chem. 282:9973-9982(2007).
CC -!- FUNCTION: Involved in the biosynthesis of the Lewis X (LeX)
CC trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the
CC addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R
CC (LacNAc-R) type II acceptor. {ECO:0000269|PubMed:12676935,
CC ECO:0000269|PubMed:16150700, ECO:0000269|PubMed:16800635,
CC ECO:0000269|PubMed:17251184, ECO:0000269|PubMed:9261149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC EC=2.4.1.152; Evidence={ECO:0000269|PubMed:12676935,
CC ECO:0000269|PubMed:16150700, ECO:0000269|PubMed:16800635,
CC ECO:0000269|PubMed:17251184, ECO:0000269|PubMed:9261149};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for Gal-beta-1-4-GlcNAc-beta-O-R
CC {ECO:0000269|PubMed:12676935};
CC KM=48 uM for GDP-fucose {ECO:0000269|PubMed:12676935};
CC Vmax=11.8 umol/min/mg enzyme toward Gal-beta-1-4-GlcNAc-beta-O-R
CC {ECO:0000269|PubMed:12676935};
CC -!- PATHWAY: Lipopolysaccharide biosynthesis; LPS oligosaccharide
CC biosynthesis. {ECO:0000303|PubMed:12676935,
CC ECO:0000303|PubMed:16150700, ECO:0000303|PubMed:16800635,
CC ECO:0000303|PubMed:17251184}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16800635}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9261149}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9261149}. Cytoplasm
CC {ECO:0000269|PubMed:9261149}. Note=Predominantly localizes at the
CC membrane. {ECO:0000269|PubMed:9261149}.
CC -!- DOMAIN: The tandem repeat region, which may form a leucine zipper
CC structure, is essential for dimerization as well as for enzyme
CC stability. {ECO:0000269|PubMed:16800635}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AF008596; AAB81031.1; -; Genomic_DNA.
DR PDB; 2NZW; X-ray; 1.90 A; A/B/C=1-363.
DR PDB; 2NZX; X-ray; 1.90 A; A/B/C=1-363.
DR PDB; 2NZY; X-ray; 2.05 A; A/B/C=1-363.
DR PDB; 5ZOI; X-ray; 3.19 A; A/B=1-412.
DR PDBsum; 2NZW; -.
DR PDBsum; 2NZX; -.
DR PDBsum; 2NZY; -.
DR PDBsum; 5ZOI; -.
DR AlphaFoldDB; O30511; -.
DR SMR; O30511; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR KEGG; ag:AAB81031; -.
DR BRENDA; 2.4.1.152; 2604.
DR BRENDA; 2.4.1.214; 2604.
DR UniPathway; UPA00301; -.
DR EvolutionaryTrace; O30511; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IMP:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR016646; Alpha-1_3/4-FUT_helico.
DR InterPro; IPR041058; FucT_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF18025; FucT_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
DR PIRSF; PIRSF016150; Alpha1_3/4FUT_helico; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Membrane; Repeat; Transferase.
FT CHAIN 1..478
FT /note="Alpha-(1,3)-fucosyltransferase FucT"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438421"
FT REPEAT 364..370
FT /note="1"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 371..377
FT /note="2"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 378..384
FT /note="3"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 385..391
FT /note="4"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 392..398
FT /note="5"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 399..405
FT /note="6"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 406..412
FT /note="7"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 413..419
FT /note="8"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 420..426
FT /note="9"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REPEAT 427..433
FT /note="10"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REGION 347..353
FT /note="Important for acceptor specificity"
FT /evidence="ECO:0000269|PubMed:12676935"
FT REGION 364..433
FT /note="10 X 7 AA tandem repeat of D-D-L-R-[IV]-N-Y"
FT /evidence="ECO:0000269|PubMed:16800635"
FT REGION 434..478
FT /note="May be involved in membrane binding"
FT /evidence="ECO:0000269|PubMed:16800635"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT BINDING 186..189
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT BINDING 222..225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT BINDING 246..250
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17251184,
FT ECO:0007744|PDB:2NZY"
FT SITE 95
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 95
FT /note="E->D: Loss of alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 195
FT /note="R->A: Loss of alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 195
FT /note="R->K: Loss of 97% alpha-(1,3)-fucosyltransferase
FT catalytic activity with a 6-fold decrease in affinity for
FT GDP-fucose and a 14-fold increase in affinity for LacNAc."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 240
FT /note="N->A: Loss of 90% alpha-(1,3)-fucosyltransferase
FT catalytic activity with an 18-fold increase in affinity for
FT LacNAc."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 246
FT /note="Y->A: Loss of 80% alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 246
FT /note="Y->F: Loss of 95% alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 249
FT /note="E->A,D,Q: Loss of alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 250
FT /note="K->A: Loss of alpha-(1,3)-fucosyltransferase
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:17251184"
FT MUTAGEN 347..353
FT /note="DNPFIFC->CNDAHYSALH: Reduced alpha-(1,3)-
FT fucosyltransferase activity characterized by a 6-fold
FT decrease in affinity and 7-fold decrease in catalytic
FT efficiency. Acquires alpha-(1,4)-fucosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:12676935"
FT MUTAGEN 350
FT /note="F->Y,A: No effect on alpha-(1,3)-fucosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16150700"
FT MUTAGEN 352
FT /note="F->A: 75 percent reduction in alpha-(1,3)-
FT fucosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16150700"
FT MUTAGEN 352
FT /note="F->Y: No effect on alpha-(1,3)-fucosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16150700"
FT MUTAGEN 456..478
FT /note="Missing: Probably no major loss of alpha-(1,3)-
FT fucosyltransferase catalytic activity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:16800635,
FT ECO:0000269|PubMed:17251184"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5ZOI"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2NZW"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5ZOI"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:2NZW"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2NZY"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5ZOI"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2NZW"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2NZX"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2NZX"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2NZW"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:2NZW"
SQ SEQUENCE 478 AA; 56070 MW; ACD47A9C7D2D3266 CRC64;
MFQPLLDAYV ESASIEKMAS KSPPPLKIAV ANWWGDEEIK EFKNSVLYFI LSQRYTITLH
QNPNEFSDLV FGNPLGSARK ILSYQNAKRV FYTGENESPN FNLFDYAIGF DELDFNDRYL
RMPLYYDRLH HKAESVNDTT APYKLKDNSL YALKKPSHCF KEKHPNLCAV VNDESDPLKR
GFASFVASNP NAPIRNAFYD ALNSIEPVTG GGSVRNTLGY NVKNKNEFLS QYKFNLCFEN
TQGYGYVTEK IIDAYFSHTI PIYWGSPSVA KDFNPKSFVN VHDFKNFDEA IDYIKYLHTH
KNAYLDMLYE NPLNTLDGKA YFYQNLSFKK ILAFFKTILE NDTIYHDNPF IFCRDLNEPL
VTIDDLRVNY DDLRVNYDDL RINYDDLRVN YDDLRINYDD LRVNYDDLRV NYDDLRINYD
DLRVNYDDLR VNYERLLSKA TPLLELSQNT TSKIYRKAYQ KSLPLLRAIR RWVKKLGL
