| IED ID | IndEnz0001000311 |
| Enzyme Type ID | amylase000311 |
| Protein Name |
Neopullulanase 2 EC 3.2.1.135 Alpha-amylase II TVA II |
| Gene Name | tvaII |
| Organism | Thermoactinomyces vulgaris |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Thermoactinomycetaceae Thermoactinomyces Thermoactinomyces vulgaris |
| Enzyme Sequence | MLLEAIFHEAKGSYAYPISETQLRVRLRAKKGDVVRCEVLYADRYASPEEELAHALAGKAGSDERFDYFEALLECSTKRVKYVFLLTGPQGEAVYFGETGFSAERSKAGVFQYAYIHRSEVFTTPEWAKEAVIYQIFPERFANGDPSNDPPGTEQWAKDARPRHDSFYGGDLKGVIDRLPYLEELGVTALYFTPIFASPSHHKYDTADYLAIDPQFGDLPTFRRLVDEAHRRGIKIILDAVFNHAGDQFFAFRDVLQKGEQSRYKDWFFIEDFPVSKTSRTNYETFAVQVPAMPKLRTENPEVKEYLFDVARFWMEQGIDGWRLDVANEVDHAFWREFRRLVKSLNPDALIVGEIWHDASGWLMGDQFDSVMNYLFRESVIRFFATGEIHAERFDAELTRARMLYPEQAAQGLWNLLDSHDTERFLTSCGGNEAKFRLAVLFQMTYLGTPLIYYGDEIGMAGATDPDCRRPMIWEEKEQNRGLFEFYKELIRLRHRLASLTRGNVRSWHADKQANLYAFVRTVQDQHVGVVLNNRGEKQTVLLQVPESGGKTWLDCLTGEEVHGKQGQLKLTLRPYQGMILWNGR |
| Enzyme Length | 585 |
| Uniprot Accession Number | Q08751 |
| Absorption | |
| Active Site | ACT_SITE 325; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P38940; ACT_SITE 354; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P38940 |
| Activity Regulation | |
| Binding Site | BINDING 244; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 323; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 465; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 469; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).; EC=3.2.1.135; Evidence={ECO:0000269|PubMed:7763540}; |
| DNA Binding | |
| EC Number | 3.2.1.135 |
| Enzyme Function | FUNCTION: Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose. {ECO:0000269|PubMed:7763540}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (37); Binding site (4); Chain (1); Helix (27); Metal binding (6); Region (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (16) |
| Cross Reference PDB | 1BVZ; 1G1Y; 1JF5; 1JF6; 1JI2; 1JIB; 1JL8; 1VB9; 1VFM; 1VFO; 1VFU; 1WZK; 1WZL; 1WZM; 2D2O; 3A6O; |
| Mapped Pubmed ID | 11226882; 11330677; 11527532; 15138257; 15182368; 16564038; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,467 |
| Kinetics | |
| Metal Binding | METAL 143; /note="Calcium"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2"; METAL 145; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2"; METAL 148; /note="Calcium"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2"; METAL 149; /note="Calcium"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2"; METAL 169; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2"; METAL 171; /note="Calcium"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI2" |
| Rhea ID | |
| Cross Reference Brenda |