| IED ID | IndEnz0018000484 |
| Enzyme Type ID | peroxidase000484 |
| Protein Name |
Alpha- 1,3 -fucosyltransferase fut-6 EC 2.4.1.- |
| Gene Name | fut-6 CEFT-3 T05A7.5 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSQIGGATCTWRYLGRFVTLGIYASVALFVWYTLVPTRSKHKDSIAINNNNADPATALIPVHTKNVVIYAATKFFGHPITTERFLATCPDVQNYCRITQEESEFDNADAVLFHNADYRGSTDKFKKMKSQRKPGVPYVLWSLESPTNDMFRPDSHMINWTMTYRTDSDVWAPYGTIVKLKNPVEVDLNAIWEGKTKTATWLASNCITQNHRFDLIKKIIDNGFEIDIWGNCGKQVSQCAGVDNQESPCVLELIKPYKFYISMENSNCKDYVTEKFWKALNDRMTIPIVLARKYYKDLGVPDSAYIAVDDYATLDEFLAHVKKVNKEKDLFLSYHQWRKEWKVIIGSGFSGWCTLCNKLQDKDYILKNPKSYKDVAWWHSFEMCNNQIASKYL |
| Enzyme Length | 392 |
| Uniprot Accession Number | G5EEE1 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by divalent metal cations. {ECO:0000269|PubMed:17369288}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.4.1.- |
| Enzyme Function | FUNCTION: Involved in the fucosylation of N-glycans (PubMed:15364955, PubMed:17369288, PubMed:23754284, PubMed:26538210, PubMed:26002521). Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the distal GlcNAc residue in N-glycans (PubMed:23754284). Catalyzes the transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288). Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288). {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284, ECO:0000269|PubMed:26002521, ECO:0000269|PubMed:26538210}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. Very low activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288}; |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284, ECO:0000269|PubMed:26002521, ECO:0000269|PubMed:26538210}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (1); Topological domain (2); Transmembrane (1) |
| Keywords | Glycoprotein;Glycosyltransferase;Golgi apparatus;Membrane;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21085631; 22560298; 23800452; 25487147; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,226 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |