| IED ID | IndEnz0018001377 |
| Enzyme Type ID | peroxidase001377 |
| Protein Name |
Alpha- 1,3 -fucosyltransferase fut-1 EC 2.4.1.214 Fucosyltransferase fut-1 |
| Gene Name | fut-1 CEFT-1 K08F8.3 |
| 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 | MTARSIKLFFARWKYLMFACCITYLLVIYAPISKSEQKDWKEGEIELSNDHELDVPILQKEELKPQQRPSFEENVPKKKTFNFNPVGKEPFDVEEVLTSSDIKLEERMTATVIPGQKRLILSWNAGHSQDNLQGCPDWNCEFTQVRARAPDADAVLIAHMDNDFVPKPNQYVVYFSQESPANSGIQIPRPDYINMTLGFRHDTPAGSPYGYTVKLGAKSRKTGQVVDANLVNGKAKGAAWFVSHCQTNSKREDFVKKLQKHLQIDIYGGCGPMKCARGDSKCDTMLDTDYHFYVTFENSICEDYVTEKLWKSGYQNTIIPLVLKRKLVEPFVPPNSFIAIDDFKSVKEMGDYLNYLMNNKTAYMEYFEWRHDYKVVFLDGSHHDVLERPWGFCQVCRMAWTEPRQKVLIPNWDAYWRQTCEKDGTLVDSIPLD |
| Enzyme Length | 433 |
| Uniprot Accession Number | G5EDR5 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Cu(2+) or Zn(2+) and to a lesser extent Ni(2+) ions. {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N(4)-{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 + H(+) + N(4)-{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)-[(1->4)-alpha-L-Fuc]-beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:24444, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13529, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60651, ChEBI:CHEBI:137182; EC=2.4.1.214; Evidence={ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224}; |
| DNA Binding | |
| EC Number | 2.4.1.214 |
| Enzyme Function | FUNCTION: Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the first GlcNAc residue (with or without alpha 1,6-linked fucose), next to the peptide chains in N-glycans (PubMed:15364955, PubMed:9675224, PubMed:17369288, PubMed:21515584). Unlike in mammals, does not require the prior action of N-acetylglucosaminyltransferase I to generate complex N-glycans (PubMed:15364955). {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. No detectable activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288}; |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:9675224}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (2); Mutagenesis (5); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Glycoprotein;Glycosyltransferase;Golgi apparatus;Magnesium;Manganese;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 (PubMed:17369288, PubMed:21515584). Glycosylation is important for enzymatic activity (PubMed:21515584). {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 21085631; 21177967; 21367940; 22267497; 22286215; 22560298; 23754284; 23800452; 24884423; 25487147; 26002521; 26538210; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,004 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for GDP-fucose (at pH 7.5 and 23 degrees Celsius) {ECO:0000269|PubMed:21515584}; KM=400 uM for Man-alpha-1-6(Man-alpha-1-3)Man-alpha-1-6(Man-alpha-1-3)Man-beta-1-4GlcNAc-beta-1-4GlcNAc (at pH 7.5 and 23 degrees Celsius) {ECO:0000269|PubMed:21515584}; |
| Metal Binding | |
| Rhea ID | RHEA:24444 |
| Cross Reference Brenda | 2.4.1.214; |