Detail Information for IndEnz0009000091
IED ID IndEnz0009000091
Enzyme Type ID chitinase000091
Protein Name Probable chitinase 10
EC 3.2.1.14
Probable chitinase 1
Probable chitinase 3
Gene Name Cht10 Cht1 Cht3 CG18140
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MHPYVPSVLVVVVLAISVKAHIRVDKLQIHSESNYKPAFIRSAVESIPLDIDAILLLRNSTKPEFGDAFLPLRSAVESIPKLYQSNTSRFRKNPDVRSFVRDSVESLPNDEDGLEHIEIFTKYYNSVSDVAGVDLKSKKLTHVNLDPGTISDKYAAFIARGNSEDYYPKSYRAGSPHQELLKMMNIEHTDKLDRYSDLQHQQSYGALGLANRNDLKMTKKVLCYMSNWAFYRSGEAHFVPEQIDPNLCSAIIYSFASLDPDHLTIREFDSWVDLDNQYYRRVTSLGVPVLIALGGWTDSSGSKYSRLVSDNLKRRVFISSVSSFLLRHGFSGLHLDWNYPKCWQSDCSRGPVTDRPNLTKLLRELRTEFQSVDPKFQLGVAISGYKEIIKEAYDFPALSDIVDYMTVMTYDYHGAWEQKTGHVSPLYGLSSDTYPQYNTNYTMQLLLKMGARREKLVLSIPFYGQSFTLATAHQILAGPGVAASGPGDAGELTKQPGMLAYYEICQRLTKFNWISDRNLNVIFGPFAMLNDQWVGYEDPTSAQAKARYAANNNFAGVAAWTIDLDDFRNLCCNESYPLLRAINRALGRLDSEPPTQPNCKRPTLLATPVPPQMTTISSDGSGGLGQNHDHTTSLPSGQISSSPVSTTITSTFPWWSSTTKRPREPTKTTAQPTHTTILIPAGINPVVQPSNCKSGEFFADSNNCNAYYHCFFAGELQQQFCPSGLHWNNEAKGCDWPSSAQCSLKLDQHLSTSYPNPIQTSKKPETTLKPNKKPSEISTHHQVNSTSSRPQYMRPTILECTEGDYYPHRNCRKYYICVNKALVPSECGGDLHWDGIKKLCDWPENVQCVTSKKYLKIIKSSSANEEDPCKGEKRVPYPGNCSKYLFCLWNRLQASDCPPGLHYNERIGNCDWPAAAKCNPKGSESSEEAELNAMPKPPTPQTPSSHLRPTYPTEKPVPKPRDSHYKVICYFTNWAWYRKGIGRFTPDDINTELCTHVIYGFAVLDYSELVLRTHDSWADVENNFYTRVTSLKSKGIKVSLALGGWNDSQGDKYSRLVRSPMARSRFVRHALEFIEKYGFEGLDLDWEYPVCWQTECNKGSTEEKDGFTAWVQELSEAFRPRGLMLSTAVSPSRKIIDAGYDIPQLSRYFDWIAVMTYDFHGHWDKKTGHVAPLYHHPDDDFEYFNVNYSINYWMEKGAPSQKLVMGIPLYGQSFTLENTNSSGLNAKAPAPGEAGEFTRAAGFLAYYEICERVNRQGWQVVHDEFGRMGPYAYKGTQWVSYDSPDMVRKKSLLVRSLKLGGGMVWALDLDDFKNRCGNGVHPLLTEIHNVLKDPPSLMEIPGPIETTPTEYPGMEEEIHESNGEGPEVQPIEAVMQTCENEGEEHEGILDPNHVLEEENIEATEMATEFKIICYFTNWAWYRQGGGKFLPEDIDSDLCTHIIYGFAVLSRDNLTIQPHDSWADLDNKFYERIVAYRKKGAKVTVAIGGWNDSAGDKYSRLVRNPEARSRFIRNVLDFIEEYNFDGLDLDWEYPVCWQVDCKKGTAEEKIGFSALVRELFYAFQPRGLILSAAVSPNKKVIDAGYEVAELSHYFSWISVMAYDYHGQWDKKTGHVAPMYSHPEGTANFNANFSMNYWISMGADRRKLVMGIPLYGQSFSLAETTKHQLNAPTYGGGEAGEATRARGFLAYYEICLKIRHHRWNVVRDTKGRIGPFAYHGDQWVSFDDVPMIRHKSEYIKAMGLGGAMIWALDLDDFKNVCECESYPLLKAINRVLRGFGGPQPKCLLENPKSTMKPNIKPPFRPTINAPSGPNLDSPTQNVSLNVLSIKCHSKNYLAHEWDCTKYYICEHGTYVERSCPLGLQWNKTYCDWPTNVQSSLGSNQRTQEPAVHRPNPTSVITEPPIINNSYKVVCYFTSWAWYRSSQGKFVPEDIDANLCTHLIYGFAVLDSKSLTIKTHDSWTDIDNRFYERVVEYKQRGLRVMLAIGGWNDSLGSKYARLVLNSQSRRRFVASVISFLEQHGFEGLDLAWEFPVCWQVNCNRGNPTEKDGFVALVKELSEAFKENGLILSAAVSPSKMVIDAGYNVFELSPYFDWVAVMTYDFHGHWDMRTGQIAPLFHRGGDENLYLNGNFSIHYWLERGIPNDKLVMGMPMYGQTFTLADQNRRSLNDKTVGPGKAGTFTRADGFLAYYEICEKVVNDDWKVVRDEEGIFGSYAYSGNQWISYDDVTTIRRKSQFIKSLQLGGGMIWALDLDDFRGLCGCGKHPLLRTLSQELLGIPGQKAKDCI
Enzyme Length 2286
Uniprot Accession Number Q9W5U2
Absorption
Active Site ACT_SITE 1087; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; ACT_SITE 1531; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; ACT_SITE 2030; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Activity Regulation
Binding Site BINDING 339; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 560; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 1088; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 1305; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 1532; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 1748; /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
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Binding site (6); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (8); Erroneous initiation (1); Region (12); Signal peptide (1)
Keywords Carbohydrate metabolism;Chitin degradation;Chitin-binding;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11914129; 12537574; 12654931; 12723700; 14630943; 14734306; 15520262; 15612038; 15883367; 16033869; 17110485; 17154718; 17594485; 18208336; 18342250; 18342251; 19232407; 21611131; 22590528; 22761891; 23071443; 24077308; 26097463; 26656493; 26801178; 26838602; 27357258; 27513559; 27582081; 29237855; 29670218; 31036678; 31722958; 32129536; 32770153; 33540716;
Motif
Gene Encoded By
Mass 258,777
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda