IED ID | IndEnz0001000310 |
Enzyme Type ID | amylase000310 |
Protein Name |
Neopullulanase 1 EC 3.2.1.135 Alpha-amylase I TVA I |
Gene Name | tvaI |
Organism | Thermoactinomyces vulgaris |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Thermoactinomycetaceae Thermoactinomyces Thermoactinomyces vulgaris |
Enzyme Sequence | MIKLLKPMSLSILLVFILSFSFPFPTAKAAANDNNVEWNGLFHDQGPLFDNAPEPTSTQSVTLKLRTFKGDITSANIKYWDTADNAFHWVPMVWDSNDPTGTFDYWKGTIPASPSIKYYRFQINDGTSTAWYNGNGPSSTEPNADDFYIIPNFKTPDWLKNGVMYQIFPDRFYNGDSSNDVQTGSYTYNGTPTEKKAWGSSVYADPGYDNSLVFFGGDLAGIDQKLGYIKKTLGANILYLNPIFKAPTNHKYDTQDYMAVDPAFGDNSTLQTLINDIHSTANGPKGYLILDGVFNHTGDSHPWFDKYNNFSSQGAYESQSSPWYNYYTFYTWPDSYASFLGFNSLPKLNYGNSGSAVRGVIYNNSNSVAKTYLNPPYSVDGWRLDAAQYVDANGNNGSDVTNHQIWSEFRNAVKGVNSNAAIIGEYWGNANPWTAQGNQWDAATNFDGFTQPVSEWITGKDYQNNSASISTTQFDSWLRGTRANYPTNVQQSMMNFLSNHDITRFATRSGGDLWKTYLALIFQMTYVGTPTIYYGDEYGMQGGADPDNRRSFDWSQATPSNSAVALTQKLITIRNQYPALRTGSFMTLITDDTNKIYSYGRFDNVNRIAVVLNNDSVSHTVNVPVWQLSMPNGSTVTDKITGHSYTVQNGMVTVAVDGHYGAVLAQ |
Enzyme Length | 666 |
Uniprot Accession Number | Q60053 |
Absorption | |
Active Site | ACT_SITE 385; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P38940; ACT_SITE 425; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P38940 |
Activity Regulation | |
Binding Site | BINDING 296; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 383; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 545; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 549; /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:7548164}; |
DNA Binding | |
EC Number | 3.2.1.135 |
Enzyme Function | FUNCTION: Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Also hydrolyzes cyclodextrins. {ECO:0000269|PubMed:7548164}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (36); Binding site (4); Chain (1); Helix (25); Metal binding (16); Region (1); Signal peptide (1); Site (1); Turn (14) |
Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Chloride;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..29 |
Structure 3D | X-ray crystallography (11) |
Cross Reference PDB | 1IZJ; 1IZK; 1JI1; 1UH2; 1UH3; 1UH4; 2D0F; 2D0G; 2D0H; 5Z0T; 5Z0U; |
Mapped Pubmed ID | 12860426; 14687576; 16302977; |
Motif | |
Gene Encoded By | |
Mass | 74,296 |
Kinetics | |
Metal Binding | METAL 31; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 33; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 35; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 71; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 125; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 174; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 176; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 179; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 180; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 216; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 218; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 305; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 309; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 310; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 312; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1"; METAL 317; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12051850, ECO:0007744|PDB:1JI1" |
Rhea ID | |
Cross Reference Brenda |