Detail Information for IndEnz0001000380
IED ID IndEnz0001000380
Enzyme Type ID amylase000380
Protein Name Malto-oligosyltrehalose trehalohydrolase
MTHase
EC 3.2.1.141
4-alpha-D-
1-
4
-alpha-D-glucano
trehalose trehalohydrolase
Maltooligosyl trehalose trehalohydrolase
Gene Name treZ
Organism Arthrobacter sp. (strain Q36)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Micrococcaceae Arthrobacter unclassified Arthrobacter Arthrobacter sp. (strain Q36)
Enzyme Sequence MTHTYPREAAKPVLGPARYDVWAPNAESVTLLAGGERYAMQRRAETGPEDAGWWTAAGAPTDGNVDYGYLLDGDETPLPDPRTRRQPDGVHALSRTFDPSAYSWQDDAWQGRELQGAVIYELHLGTFTPEGTLEAAAGKLDYLAGLGVDFIELLPVNAFNGTHNWGYDGVQWFAVHEAYGGPEAYQRFVDAAHAAGLGVIQDVVYNHLGPSGNYLPRFGPYLKQGEGNTWGDSVNLDGPGSDHVRRYILDNLAMWLRDYRVDGLRLDAVHALKDERAVHILEDFGALADQISAEVGRPLTLIAESDLNNPRLLYPRDVNGYGLEGQWSDDFHHAVHVNVTGETTGYYSDFDSLAALAKVLRDGFFHDGSYSSFRERHHGRPINFSAVHPAALVVCSQNHDQIGNRATGDRLSQTLPYGSLALAAVLTLTGPFTPMLLMGEEYGASTPWQFFTSHPEPELGKATAEGRIKEFERMGWDPAVVPDPQDPETFRRSKLDWAEAAEGDHARLLELYRSLTALRRSTPDLTKLGFEDTQVAFDEDARWLRFRRGGVQVLLNFSEQPVSLDGAGTALLLATDDAVRLEGERAELGPLSAAVVSD
Enzyme Length 598
Uniprot Accession Number Q44316
Absorption
Active Site ACT_SITE 267; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q55088; ACT_SITE 304; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q55088
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.; EC=3.2.1.141; Evidence={ECO:0000250|UniProtKB:Q55088};
DNA Binding
EC Number 3.2.1.141
Enzyme Function
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
nucleotide Binding
Features Active site (2); Chain (1); Region (3); Site (1)
Keywords Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 65,832
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda