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 |