| IED ID | IndEnz0018000483 |
| Enzyme Type ID | peroxidase000483 |
| Protein Name |
Alpha- 1,3 -fucosyltransferase fut-5 EC 2.4.1.65 Fucosyltransferase fut-5 |
| Gene Name | fut-5 CEFT-2 T05A7.10 |
| 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 | MKHNTLRAVFQFSFFIGICTFIMIAGYSYQINYNQRMGIFYGGNITFKKVPKVVIYTATPFFDVPIENSILRDCSEKIKNSCTVTSNNKTFPIADAIVFHSRDINETKLSFFNKNRRYDIPYIMMAMENPFFAGLTVYHNFFNWTMTYRTDSDIFHPYGAFVKSYVPAEVNYSEIWNSKTKETLWMVSNGNAQNKRKELVEKLIKKGMSIDLYGQLYKKEPAECPRRRGPPGCDVKFHSPYKFAIAFENSNCKDYVTEKFWKKAGIYKTVPIVMSRKIYRDLGIPDSMYIAVDDYPNLEEFVHHIQNVTSNEEEYMKYHKWRKQFKIVDTNEGNIGFCQLCQKLAGYKRKLVPHKVYENLNSWHSTSTCDNSFATRFL |
| Enzyme Length | 378 |
| Uniprot Accession Number | G5EE06 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Cu(2+) and Ni(2+), and to a lesser extent by EDTA, Mn(2+) and Mg(2+). {ECO:0000269|PubMed:17369288}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304; EC=2.4.1.65; Evidence={ECO:0000269|PubMed:17369288}; |
| DNA Binding | |
| EC Number | 2.4.1.65 |
| Enzyme Function | FUNCTION: Catalyzes the addition of fucose in alpha 1-3 linkage to GalNAc-beta-1->4-GlcNAc-beta-1->3-Gal-beta-1->4-Glc (LDNT)acceptor. Unlike fut-1, does not add 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) or 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) acceptors. {ECO:0000269|PubMed:17369288}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. Vey low activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288}; |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:17369288}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (6); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Glycoprotein;Glycosyltransferase;Golgi apparatus;Membrane;Metal-binding;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 | PTM: N-glycosylated. {ECO:0000269|PubMed:17369288}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21085631; 21367940; 22560298; 23800452; 25487147; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,346 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23628 |
| Cross Reference Brenda |