IED ID | IndEnz0011000437 |
Enzyme Type ID | glucanase000437 |
Protein Name |
Xyloglucan endotransglucosylase/hydrolase 1 EC 2.4.1.207 |
Gene Name | XTH1 EXT XTH |
Organism | Glycine max (Soybean) (Glycine hispida) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Glycine Glycine subgen. Soja Glycine max (Soybean) (Glycine hispida) |
Enzyme Sequence | MGSSSSMWTVCVILASLASAALCANPRRPVDVQFGRNYVPTWAFDHIKYFNGGSDIQPHLDKYTGTGFQPKGSYLFGHFSMYIKMVPGDSAGTVTAFYLSSQNAEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIYLWFDPTKEYHRYSILWNLYQIVFFVDEVPIRVFKNSKDLGVKFPFDQPMKIYNSLWNADDWATRGGLEKTDWSKAPFIAAYKGFHIDGCEASVNAKFCDTQGKRWWDQPEFRDLDAAQWRRLRWVRQKYTIYNYCTDTKRYPHISPPECKRDRDI |
Enzyme Length | 296 |
Uniprot Accession Number | Q39857 |
Absorption | |
Active Site | ACT_SITE 108; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10064; ACT_SITE 112; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10064 |
Activity Regulation | |
Binding Site | BINDING 112; /note=Xyloglucan; /evidence=ECO:0000250|UniProtKB:Q8GZD5; BINDING 206; /note=Xyloglucan; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q8GZD5; BINDING 281; /note=Xyloglucan; /evidence=ECO:0000250|UniProtKB:Q8GZD5 |
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:0000250|UniProtKB:Q38857}; |
DNA Binding | |
EC Number | 2.4.1.207 |
Enzyme Function | FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. {ECO:0000250|UniProtKB:Q38857}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (3); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Region (3); Sequence conflict (4); Signal peptide (1); Site (1) |
Keywords | Apoplast;Cell wall;Cell wall biogenesis/degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal;Transferase |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted, extracellular space, apoplast {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000250|UniProtKB:Q38857}.; PTM: N-glycosylated; not essential for its enzymatic activity. {ECO:0000250|UniProtKB:Q9ZSU4}. |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,435 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |