Detail Information for IndEnz0001000311
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