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Entry version 82 (16 Oct 2019)
Sequence version 1 (01 Jan 1998)
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Protein

Alpha-(1,3)-fucosyltransferase FucT

Gene

fucT

Organism
Helicobacter pylori (Campylobacter pylori)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor.5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.31 mM for Gal-beta-1-4-GlcNAc-beta-O-R1 Publication
  2. KM=48 µM for GDP-fucose1 Publication
  1. Vmax=11.8 µmol/min/mg enzyme toward Gal-beta-1-4-GlcNAc-beta-O-R1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: LPS oligosaccharide biosynthesis

This protein is involved in the pathway LPS oligosaccharide biosynthesis, which is part of Lipopolysaccharide biosynthesis.4 Publications
View all proteins of this organism that are known to be involved in the pathway LPS oligosaccharide biosynthesis and in Lipopolysaccharide biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei94Substrate; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei95Important for catalytic activity1 Publication1
Binding sitei195SubstrateCombined sources1 Publication1
Binding sitei240SubstrateCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.214 2604

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00301

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT10 Glycosyltransferase Family 10

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-(1,3)-fucosyltransferase FucT1 Publication (EC:2.4.1.1525 Publications)
Alternative name(s):
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferaseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:fucTImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHelicobacter pylori (Campylobacter pylori)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri210 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi95E → D: Loss of alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi195R → A: Loss of alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi195R → K: Loss of 97% alpha-(1,3)-fucosyltransferase catalytic activity with a 6-fold decrease in affinity for GDP-fucose and a 14-fold increase in affinity for LacNAc. 1 Publication1
Mutagenesisi240N → A: Loss of 90% alpha-(1,3)-fucosyltransferase catalytic activity with an 18-fold increase in affinity for LacNAc. 1 Publication1
Mutagenesisi246Y → A: Loss of 80% alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi246Y → F: Loss of 95% alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi249E → A, D or Q: Loss of alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi250K → A: Loss of alpha-(1,3)-fucosyltransferase catalytic activity. 1 Publication1
Mutagenesisi347 – 353DNPFIFC → CNDAHYSALH: Reduced alpha-(1,3)-fucosyltransferase activity characterized by a 6-fold decrease in affinity and 7-fold decrease in catalytic efficiency. Acquires alpha-(1,4)-fucosyltransferase activity. 1 Publication7
Mutagenesisi350F → Y or A: No effect on alpha-(1,3)-fucosyltransferase activity. 1 Publication1
Mutagenesisi352F → A: 75 percent reduction in alpha-(1,3)-fucosyltransferase activity. 1 Publication1
Mutagenesisi352F → Y: No effect on alpha-(1,3)-fucosyltransferase activity. 1 Publication1
Mutagenesisi456 – 478Missing : Probably no major loss of alpha-(1,3)-fucosyltransferase catalytic activity. No effect on dimerization. 2 PublicationsAdd BLAST23

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004384211 – 478Alpha-(1,3)-fucosyltransferase FucTCuratedAdd BLAST478

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O30511

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O30511

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati364 – 37011 Publication7
Repeati371 – 37721 Publication7
Repeati378 – 38431 Publication7
Repeati385 – 39141 Publication7
Repeati392 – 39851 Publication7
Repeati399 – 40561 Publication7
Repeati406 – 41271 Publication7
Repeati413 – 41981 Publication7
Repeati420 – 42691 Publication7
Repeati427 – 433101 Publication7

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni186 – 189Substrate bindingCombined sources1 Publication4
Regioni222 – 225Substrate bindingCombined sources1 Publication4
Regioni246 – 250Substrate bindingCombined sources1 Publication5
Regioni347 – 353Important for acceptor specificity1 Publication7
Regioni364 – 43310 X 7 AA tandem repeat of D-D-L-R-[IV]-N-Y1 PublicationAdd BLAST70
Regioni434 – 478May be involved in membrane binding1 PublicationAdd BLAST45

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The tandem repeat region, which may form a leucine zipper structure, is essential for dimerization as well as for enzyme stability.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyltransferase 10 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K20151

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.11650, 1 hit
3.40.50.11660, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016646 Alpha-1_3/4-FUT_helico
IPR041058 FucT_N
IPR042574 FucT_N_sf
IPR001503 Glyco_trans_10
IPR038577 GT10-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11929 PTHR11929, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18025 FucT_N, 1 hit
PF00852 Glyco_transf_10, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF016150 Alpha1_3/4FUT_helico, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O30511-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFQPLLDAYV ESASIEKMAS KSPPPLKIAV ANWWGDEEIK EFKNSVLYFI
60 70 80 90 100
LSQRYTITLH QNPNEFSDLV FGNPLGSARK ILSYQNAKRV FYTGENESPN
110 120 130 140 150
FNLFDYAIGF DELDFNDRYL RMPLYYDRLH HKAESVNDTT APYKLKDNSL
160 170 180 190 200
YALKKPSHCF KEKHPNLCAV VNDESDPLKR GFASFVASNP NAPIRNAFYD
210 220 230 240 250
ALNSIEPVTG GGSVRNTLGY NVKNKNEFLS QYKFNLCFEN TQGYGYVTEK
260 270 280 290 300
IIDAYFSHTI PIYWGSPSVA KDFNPKSFVN VHDFKNFDEA IDYIKYLHTH
310 320 330 340 350
KNAYLDMLYE NPLNTLDGKA YFYQNLSFKK ILAFFKTILE NDTIYHDNPF
360 370 380 390 400
IFCRDLNEPL VTIDDLRVNY DDLRVNYDDL RINYDDLRVN YDDLRINYDD
410 420 430 440 450
LRVNYDDLRV NYDDLRINYD DLRVNYDDLR VNYERLLSKA TPLLELSQNT
460 470
TSKIYRKAYQ KSLPLLRAIR RWVKKLGL
Length:478
Mass (Da):56,070
Last modified:January 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iACD47A9C7D2D3266
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF008596 Genomic DNA Translation: AAB81031.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAB81031

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008596 Genomic DNA Translation: AAB81031.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NZWX-ray1.90A/B/C1-363[»]
2NZXX-ray1.90A/B/C1-363[»]
2NZYX-ray2.05A/B/C1-363[»]
5ZOIX-ray3.19A/B1-412[»]
SMRiO30511
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGT10 Glycosyltransferase Family 10

Genome annotation databases

KEGGiag:AAB81031

Phylogenomic databases

KOiK20151

Enzyme and pathway databases

UniPathwayiUPA00301
BRENDAi2.4.1.214 2604

Miscellaneous databases

EvolutionaryTraceiO30511

Family and domain databases

Gene3Di3.40.50.11650, 1 hit
3.40.50.11660, 1 hit
InterProiView protein in InterPro
IPR016646 Alpha-1_3/4-FUT_helico
IPR041058 FucT_N
IPR042574 FucT_N_sf
IPR001503 Glyco_trans_10
IPR038577 GT10-like_sf
PANTHERiPTHR11929 PTHR11929, 2 hits
PfamiView protein in Pfam
PF18025 FucT_N, 1 hit
PF00852 Glyco_transf_10, 1 hit
PIRSFiPIRSF016150 Alpha1_3/4FUT_helico, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFUCT_HELPX
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O30511
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 30, 2016
Last sequence update: January 1, 1998
Last modified: October 16, 2019
This is version 82 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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