| IED ID | IndEnz0001000328 |
| Enzyme Type ID | amylase000328 |
| Protein Name |
Neopullulanase EC 3.2.1.135 |
| Gene Name | nplT |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MRKEAIYHRPADNFAYAYDSETLHLRLRTKKDDIDRVELLHGDPYDWQNGAWQFQMMPMRKTGSDELFDYWFAEVKPPYRRLRYGFVLYSGEEKLVYTEKGFYFEVPTDDTAYYFCFPFLHRVDLFEAPDWVKDTVWYQIFPERFANGNPSISPEGSRPWGSEDPTPTSFFGGDLQGIIDHLDYLVDLGITGIYLTPIFRSPSNHKYDTADYFEVDPHFGDKETLKTLIDRCHEKGIRVMLDAVFNHCGYEFAPFQDVWKNGESSKYKDWFHIHEFPLQTEPRPNYDTFRFVPQMPKLNTANPEVKRYLLDVATYWIREFDIDGWRLDVANEIDHEFWREFRQEVKALKPDVYILGEIWHDAMPWLRGDQFDAVMNYPFTDGVLRFFAKEEISARQFANQMMHVLHSYPNNVNEAAFNLLGSHDTSRILTVCGGDIRKVKLLFLFQLTFTGSPCIYYGDEIGMTGGNDPECRKCMVWDPMQQNKELHQHVKQLIALRKQYRSLRRGEISFLHADDEMNYLIYKKTDGDETVLVIINRSDQKADIPIPLDARGTWLVNLLTGERFAAEAETLCTSLPPYGFVLYAIEHW |
| Enzyme Length | 588 |
| Uniprot Accession Number | P38940 |
| Absorption | |
| Active Site | ACT_SITE 328; /note=Nucleophile; /evidence=ECO:0000305|PubMed:12547200; ACT_SITE 357; /note=Proton donor; /evidence=ECO:0000305|PubMed:12547200 |
| Activity Regulation | |
| Binding Site | BINDING 247; /note=Substrate; /evidence=ECO:0000305|PubMed:12547200; BINDING 326; /note=Substrate; /evidence=ECO:0000305|PubMed:12547200; BINDING 468; /note=Substrate; /evidence=ECO:0000305|PubMed:12547200; BINDING 472; /note=Substrate; /evidence=ECO:0000305|PubMed:12547200 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).; EC=3.2.1.135; |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (37); Binding site (4); Chain (1); Helix (24); Metal binding (5); Region (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1J0H; 1J0I; 1J0J; 1J0K; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,145 |
| Kinetics | |
| Metal Binding | METAL 147; /note="Calcium"; /evidence="ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H"; METAL 149; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H"; METAL 153; /note="Calcium"; /evidence="ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H"; METAL 172; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H"; METAL 174; /note="Calcium"; /evidence="ECO:0000269|PubMed:12547200, ECO:0007744|PDB:1J0H" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.135; |