Detail Information for IndEnz0009000223
IED ID IndEnz0009000223
Enzyme Type ID chitinase000223
Protein Name Endochitinase 1
EC 3.2.1.14
Complement-fixation antigen
CF-AG
CF-antigen
Gene Name CTS1 CIMG_02795
Organism Coccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Onygenaceae Coccidioides Coccidioides immitis (Valley fever fungus) Coccidioides immitis (strain RS) (Valley fever fungus)
Enzyme Sequence MRFLIGALLTLQTLVQASSMSSMPNSYPVPEAPAEGGFRSVVYFVNWAIYGRGHNPQDLKADQFTHILYAFANIRPSGEVYLSDTWADTDKHYPGDKWDEPGNNVYGCIKQMYLLKKNNRNLKTLLSIGGWTYSPNFKTPASTEEGRKKFADTSLKLMKDLGFDGIDIDWEYPEDEKQANDFVLLLKACREALDAYSAKHPNGKKFLLTIASPAGPQNYNKLKLAEMDKYLDFWNLMAYDFSGSWDKVSGHMSNVFPSTTKPESTPFSSDKAVKDYIKAGVPANKIVLGMPLYGRAFASTDGIGTSFNGVGGGSWENGVWDYKDMPQQGAQVTELEDIAASYSYDKNKRYLISYDTVKIAGKKAEYITKNGMGGGMWWESSSDKTGNESLVGTVVNGLGGTGKLEQRENELSYPESVYDNLKNGMPS
Enzyme Length 427
Uniprot Accession Number Q1E3R8
Absorption
Active Site ACT_SITE 171; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Activity Regulation
Binding Site BINDING 172; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 378; /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 (1); Binding site (2); Chain (1); Domain (1); Erroneous gene model prediction (5); Glycosylation (1); Region (3); Signal peptide (1)
Keywords Carbohydrate metabolism;Chitin degradation;Chitin-binding;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,398
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda