Detail Information for IndEnz0009000016
IED ID IndEnz0009000016
Enzyme Type ID chitinase000016
Protein Name Chitotriosidase-1
EC 3.2.1.14
Chitinase-1
Gene Name CHIT1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFCQGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN
Enzyme Length 466
Uniprot Accession Number Q13231
Absorption
Active Site ACT_SITE 140; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Activity Regulation
Binding Site BINDING 141; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 358; /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; Evidence={ECO:0000269|PubMed:15664516, ECO:0000269|PubMed:19725875, ECO:0000269|PubMed:7836450};
DNA Binding
EC Number 3.2.1.14
Enzyme Function FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity. {ECO:0000269|PubMed:7592832, ECO:0000269|PubMed:7836450}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (4); Beta strand (22); Binding site (2); Chain (1); Disulfide bond (3); Domain (2); Erroneous initiation (1); Glycosylation (1); Helix (16); Natural variant (5); Region (4); Signal peptide (1); Turn (6)
Keywords 3D-structure;Alternative splicing;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Lysosome;Polysaccharide degradation;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted. Lysosome. Note=A small proportion is lysosomal.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000269|PubMed:7836450
Structure 3D X-ray crystallography (22); NMR spectroscopy (1)
Cross Reference PDB 1GUV; 1HKI; 1HKJ; 1HKK; 1HKM; 1LG1; 1LG2; 1LQ0; 1WAW; 1WB0; 4WJX; 4WK9; 4WKA; 4WKF; 4WKH; 5HBF; 5NR8; 5NRA; 5NRF; 6JJR; 6JK6; 6SO0; 6ZE8;
Mapped Pubmed ID 16107886; 16110781; 19881466; 23650620; 26143917; 27111557; 29283260; 31891077; 31928006; 33078933;
Motif
Gene Encoded By
Mass 51,681
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda