Detail Information for IndEnz0011000461
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;