IED ID | IndEnz0011000461 |
Enzyme Type ID | glucanase000461 |
Protein Name |
Xyloglucan endotransglucosylase protein 34 XET protein 34 EC 2.4.1.207 PttXET16-34 PttXET16A Xyloglucan endotransglucosylase protein 16A XET protein 16A Xyloglucan endotransglucosylase/hydrolase protein 34 XTH protein 34 |
Gene Name | XTH16-34 XET16A |
Organism | Populus tremula x Populus tremuloides (Hybrid aspen) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Salicaceae Saliceae Populus (poplars) Populus tremula x Populus tremuloides (Hybrid aspen) |
Enzyme Sequence | MAAAYPWTLFLGMLVMVSGTMGAALRKPVDVAFGRNYVPTWAFDHIKYFNGGNEIQLHLDKYTGTGFQSKGSYLFGHFSMQMKLVPGDSAGTVTAFYLSSQNSEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIYLWFDPTKEFHYYSVLWNMYMIVFLVDDVPIRVFKNCKDLGVKFPFNQPMKIYSSLWNADDWATRGGLEKTDWSKAPFIASYRSFHIDGCEASVEAKFCATQGARWWDQKEFQDLDAFQYRRLSWVRQKYTIYNYCTDRSRYPSMPPECKRDRDI |
Enzyme Length | 294 |
Uniprot Accession Number | Q8GZD5 |
Absorption | |
Active Site | ACT_SITE 107; /note="Nucleophile"; /evidence="ECO:0000255|PIRSR:PIRSR005604-1, ECO:0000255|PROSITE-ProRule:PRU10064, ECO:0000305|PubMed:15020748"; ACT_SITE 111; /note="Proton donor"; /evidence="ECO:0000255|PIRSR:PIRSR005604-1, ECO:0000255|PROSITE-ProRule:PRU10064, ECO:0000305|PubMed:15020748" |
Activity Regulation | |
Binding Site | BINDING 111; /note="Xyloglucan"; /evidence="ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ"; BINDING 205; /note="Xyloglucan; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ"; BINDING 280; /note="Xyloglucan"; /evidence="ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ" |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12595718, ECO:0000269|PubMed:15020748, ECO:0000269|PubMed:15125664, ECO:0000269|PubMed:15804235, ECO:0000269|PubMed:16014999}; |
DNA Binding | |
EC Number | 2.4.1.207 |
Enzyme Function | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers (PubMed:12595718, PubMed:15020748, PubMed:16014999, PubMed:15804235, PubMed:15125664). Does not catalyze xyloglucan endohydrolysis (XEH) (PubMed:15804235). Involved in early phases of secondary (S) cell wall formation in fibers of the xylem and phloem vascular tissues of wood stems. May play a role in restructuring primary cell walls, possibly creating and reinforcing the connections between the primary and S cell wall layers (PubMed:12468728). Functions in the gelatinous (G) layers of the tension wood fibers that are involved in bending of the wood stems. May play a role in G fiber shrinking by repairing broken xyloglucan cross-links between G and S2 cell wall layers via its XET activity to maintain connections between the layers (PubMed:17504814). {ECO:0000269|PubMed:12468728, ECO:0000269|PubMed:12595718, ECO:0000269|PubMed:15020748, ECO:0000269|PubMed:15125664, ECO:0000269|PubMed:15804235, ECO:0000269|PubMed:16014999, ECO:0000269|PubMed:17504814}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:15804235}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is approximately 5.5. Loses activity rapidly at pH 4-5. {ECO:0000269|PubMed:15804235}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (3); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Mutagenesis (1); Region (3); Signal peptide (1); Site (1) |
Keywords | 3D-structure;Apoplast;Cell wall;Cell wall biogenesis/degradation;Cytoplasm;Disulfide bond;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Secreted;Signal;Transferase |
Interact With | |
Induction | INDUCTION: Down-regulated in developing tension wood at the primary walled stage. {ECO:0000269|PubMed:17504814}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12468728, ECO:0000269|PubMed:17504814}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. Cytoplasm {ECO:0000269|PubMed:12468728}. Note=Localizes to the cytoplasm of cambial cells. Localizes to the cytoplasm of xylem fibers in the early stages of secondary cell wall formation. {ECO:0000269|PubMed:12468728}. |
Modified Residue | |
Post Translational Modification | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}.; PTM: N-glycosylated. Contains N-acetylglucosamine and mannose (PubMed:15804235, PubMed:15020748). Glycosylation is not essential for its catalytic activity (PubMed:15804235). {ECO:0000269|PubMed:15020748, ECO:0000269|PubMed:15804235}. |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255|RuleBase:RU361120 |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 1UMZ; 1UN1; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,218 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for reduced xyloglucan-derived nonasaccharide as acceptor substrate (at pH 5.5 and 25 degrees Celsius) {ECO:0000269|PubMed:15804235}; Vmax=42.5 nmol/min/mg enzyme with reduced xyloglucan-derived nonasaccharide as acceptor substrate (at pH 5.5 and 25 degrees Celsius) {ECO:0000269|PubMed:15804235}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 2.4.1.207; |