Detail Information for IndEnz0009000167
IED ID IndEnz0009000167
Enzyme Type ID chitinase000167
Protein Name Killer toxin subunits alpha/beta
RF2 protein

Cleaved into: Killer toxin subunit alpha; Killer toxin subunit beta
EC 3.2.1.14
Endochitinase
Gene Name
Organism Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Kluyveromyces Kluyveromyces lactis (Yeast) (Candida sphaerica) Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Enzyme Sequence MNIFYIFLFLLSFVQGLEHTHRRGSLVKRAVCYDTDQVPLNIFFGYNRADKTDSNKNMALNIFNVFRGFLAGEGGESFYNSNGNVYGFMWVGSMVHNRGFKDNILPIMENEVKNYGIPKTLYLEYDGGGDPMKSFGIILDTTSRDTVVKAAKLWSQGKKLNSYEGSKNYQATACYLSYAYRKPIVNDNFVGTCDYFTLESGKTPADQSGINGESLQGYNPNLDFSKLSAGQPICKTIGNPPNFKPSKNSDGSCKTYKVSSGESCSSIAVKYYPLSLNDIENYNKGNYGWKGCSSLQKDYNLCVSDGSAPRPVSNPIAECGPLAPGEKYNAKCPLNACCSEFGFCGLTKDYCDKKSSTTGAPGTDGCFSNCGYGSTSNVKSSTFKKIAYWLDAKDKLAMDPKNIPNGPYDILHYAFVNINSDFSIDDSAFSKSAFLKVTSSKKIPSFGGWDFSTSPSTYTIFRNAVKTDQNRNTFANNLINFMNKYNLDGIDLDWEYPGAPDIPDIPADDSSSGSNYLTFLKLLKGKMPSGKTLSIAIPSSYWYLKNFPISDIQNTVDYMVYMTYDIHGIWEYGKANSYINCHTPRKEIEDAIKMLDKAGVKFNKVFGGVANYGRSYKMVNTNCYNYGCGFQREGGNSRDMTNTPGVLSDSEIIDIDSSDKKNDRWVDTNTDCIFMKYDGNSVVSWPKSRYDLEDMFKNYGFAGTSLWAANYFKHDEWKNDEDDNNDDTEDPFDEENVYFDVYDCKNKAGYDLDNPVYGCRLETAINIIIWNGTESVNTVLNILNDYDNYIKYYEALTRAHYDSVMEKYEKWLFEEDGYYTYYTDVDGDDIIITPPDKKKRDYIQEKYSFEKEFMMSQNMTELTEIKVNKTINFMLNGTSLAVKEYNNEKVLYKRGDIPPPGSNNRLIRNSIILDKDKEAAIASFKQYSGIELSKDSFVQRDKDKKFDLNGKHYTFMHSTILNAIVLFPNVLTNIDSDYIHHISDLIEQAHNSLGNESPDNIYEVLESVVVFMSVSEIADYTYTEGKKIKEKYDKMKKTMIVGIILGIIGGLSLFLGPIGIATSVLADFALLGADAAINGELNPSDLAFALAGLFLPVFASLGKTFKFAEALQKININKSKNFDNLNEFEKIRFFRSKLGKVKMCGS
Enzyme Length 1146
Uniprot Accession Number P09805
Absorption
Active Site ACT_SITE 495; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258
Activity Regulation
Binding Site BINDING 496; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 707; /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: The alpha subunit is a potent exochitinase. Along with the beta subunit it plays a role in the initial interaction of the toxin with sensitive cells and allow the gamma subunit (the active toxin) to gain entry into the cell.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Binding site (2); Chain (2); Disulfide bond (4); Domain (4); Glycosylation (5); Propeptide (1); Region (3); Signal peptide (1)
Keywords Carbohydrate metabolism;Chitin degradation;Chitin-binding;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Plasmid;Polysaccharide degradation;Reference proteome;Repeat;Signal;Toxin
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: RF2 is potentially split by membrane-bound basic amino acid-specific peptidase to yield the alpha and beta subunits.
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By Plasmid pGKl-1
Mass 128,937
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda