Detail Information for IndEnz0009000118
IED ID IndEnz0009000118
Enzyme Type ID chitinase000118
Protein Name Endochitinase
EC 3.2.1.14
MF1 antigen
Gene Name
Organism Brugia malayi (Filarial nematode worm)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Spirurina Spiruromorpha Filarioidea Onchocercidae Brugia Brugia malayi (Filarial nematode worm)
Enzyme Sequence MNRTTLILFFIILSNTITVIHGYVRGCYYTNWAQYRDGEGKFLPGNIPNGLCTHILYAFAKVDELGDSKPFEWNDEDTEWSKGMYSAVTKLRETNPGLKVLLSYGGYNFGSAIFTGIAKSAQKTERFIKSAIAFLRKNNFDGFDLDWEYPVGVAEEHAKLVEAMKTAFVEEAKTSGKQRLLLTAAVSAGKGTIDGSYNVESLGKNFDLLFLMSYDLHGSWEKNVDLHGKLHPTKGEVSGIGIFNTEFAADYWASKGMPKEKIIIGIPMYAQGWTLDNPSETAIGAAASRPSSASKTNPAGGTASYWEICKYLKEGGKETVHQEGVGAYMVKGDQWYGYDNEETIRIKMKWLKEKGYGGAFIWALDFDDFTGKSCGKGPYPLLNAISSELEGESENPEITTEEPSITETEAYETDETEETSETEAYDTDETEETSETEATTYDTDETEGQECPERDGLFPHPTDCHLFIQCANNIAYVMQCPATTFFNDAIKVCDHMTNAPDTCI
Enzyme Length 504
Uniprot Accession Number P29030
Absorption
Active Site ACT_SITE 148; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Activity Regulation
Binding Site BINDING 149; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 362; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
DNA Binding
EC Number 3.2.1.14
Enzyme Function FUNCTION: Microfilarial chitinase, which may function to degrade chitin-containing structures in the micro-filaria or in its mosquito vector during parasite development and transmission.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Binding site (2); Chain (1); Compositional bias (2); Disulfide bond (2); Domain (2); Region (5); Repeat (3); Signal peptide (1)
Keywords Calcium;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: O-glycosylated.
Signal Peptide SIGNAL 1..22
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 55,971
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.14;