Detail Information for IndEnz0001000908
IED ID IndEnz0001000908
Enzyme Type ID amylase000908
Protein Name Amylopullulanase
Alpha-amylase/pullulanase

Includes: Alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
; Pullulanase
EC 3.2.1.41
1,4-alpha-D-glucan glucanohydrolase
Alpha-dextrin endo-1,6-alpha-glucosidase
Gene Name apu
Organism Thermoanaerobacter thermohydrosulfuricus (Clostridium thermohydrosulfuricum)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacteraceae Thermoanaerobacter Thermoanaerobacter thermohydrosulfuricus (Clostridium thermohydrosulfuricum)
Enzyme Sequence MFKRRALGFLLAFLLVFTAVFGSMPMEFAKAETDTAPAIANVVGNFQSKLGDSDWNINSDKTIMTYKGNGFYEFTTPVALPAGDYEYKVALNHSWEGGGVPSQGNLSFHLDSDSVVTFYYNYNTSSITDSTKYTPIPEDKLPRLVGTIQPAIGAGDDWKPETSTAIMRDYKFNNVYEYTANVPKGNYEFKVTLGPSWDINYGLNGEQNGPNIPLNVAYDTKITFYYDSVSHNIWTDYNPPLTGPDNNIYYDDLRHDTHDPFFRSPFGAIKTGDTVTLRIQAKNHDIESAKISYWDDIKKTRIEVPMYRIGQSPDGKYEYWEVKLSFDHPTRIWYYFILKDGTKTAYYGDNDEQLGGVGKATDTENKDFELTVYDKNLDTPDWMKGSVMYQIFPDRFFNGDSSNDHLKKYSRGFDPVEYHSNWYELPDNPNDKNKLGYTGDGIWSNDFFGGDLKGIDDKLDYLKSLGISVIYLNPIFQSPSNHRYDTTDYTKIDELLGDLSTFKKLMEDAHAKGIKVILDGVFNHTSDDSIYFDRYGKYLNTGVLGAYQAWKQGDQSKSPYGDWYEIKPDGTYEGWWGFDSLPVIRQINGSEYNVKSWADFIINNPNAISKYWLNPDGDKNVGADGWRLDVANEVAHDFWVHFRGAINTVKPNAPMVAENWNDASLDLLGDSFNSVMNYLFRNAVIDFILDKSFDDGNVVHNPIDAAKLDQRLMSIYERYPLPVFYSTMNLLGSHDTMRILTVFGYNSADENQNSQAAKDLAVKRLKLAAILQMGYPGMPSIYYGDEAGQSGGKDPDNRRTFPWGREDTDLQTFFKKVVNIRNENQVLKTGDLETLYANGDVYAFGRRIINGKDTFGKSYPDSVAIVVINKGDAKQVSIDTTKFIRDGVAFTDALSGKTYTVQDGKIVVEVGSMDGAILISDTGQNLTAPQPITDLKAVSGNGKVDLSWSVVDKAVSYNIYRSTVKGGLYEKIASNVTQITYTDTEVTNGLKYVYAVTAVDNDGNESALSNEVEAYPAFPIGWAGNMNQVNTHVIGVNNPVEVYAEVWAQGLTDKPGQGENMIAQLGYRYIGDTVGDAVYNAVYNKVEGVEISKDWTWVDAQYVGDSGNNDKYMAKFVPDMVGTWEYIMRFSSNQGHDWTYTKGPDGKTDEAKQFTVVPSNDVETPTAPVLQQPGIESSRVTLNWSPSADDVAIFGYEIYKSSSETGPFIKIATVSDSVYNYVDTDVVNGNVYYYKVVAVDTSYNRTASNTVKATPDIIPIKVTFNVTIPDYTPDDGVNIAGNFPDAFWNPNANQMTKAGSNTYSITLTLNEGTQIEYKYARGSWDKVEKGEYGNEIDNRKITVVNQGSNTMVVNDTVQRWRDVPIYIYSPKDKTIVDANTSEIEIKGNTYKGAKVTINDESFVQQENGVFTKVVPLEYGVNTIKIHVEPSGDKNNELTKDITITVTREKPARRQNLLLLHQQKQQNHLKKYHKAK
Enzyme Length 1475
Uniprot Accession Number P16950
Absorption
Active Site ACT_SITE 629; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q60053; ACT_SITE 658; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q60053
Activity Regulation
Binding Site BINDING 524; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 627; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 794; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 798; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41;
DNA Binding
EC Number 3.2.1.1; 3.2.1.41
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (4); Chain (1); Domain (3); Metal binding (10); Region (1); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000269|PubMed:3260488
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 165,631
Kinetics
Metal Binding METAL 245; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 247; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 285; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 340; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 398; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 400; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 403; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 404; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 449; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 451; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053
Rhea ID
Cross Reference Brenda