| IED ID | IndEnz0001000550 |
| Enzyme Type ID | amylase000550 |
| 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 | Thermoanaerobacterium saccharolyticum |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Thermoanaerobacterium Thermoanaerobacterium saccharolyticum |
| Enzyme Sequence | MYKKLFTKKFISFVMSLLLVLTAAFSSMPFHNVYAADNASVVANIVGDFQDQLGDSNWNIDSNITIMQYVGNGLYEFTTPTQLKAGSYQYKVALNHSWNGGGVPSQGNLTLNLTNDSYVTFWFDYNTQSVTDSTKYTPISNDKLPRLVGTIQSAIGAGKDWDPGTSTAIMIDDNFDNVYSYTAHIPKGDYQYKVTLGNTWAENYGANGVQDGSNIQLSVANDADITFFYDANTHNIWTNYSPTLTGLDNNIYYDDLKHDTHDPFFRNPFGAIKVGQTVTLRIQAKNHDLESARISYWDDINKTRTELPMTRIGESPDGNYEYWEIKLSFDHPTRIWYYFILKDGTKTAYYGDNDDQLGGLGKATDTVNKDFELTVYDKNFDTNDWMKGAVMYQIFPDRFYNGDTSNDHAKTLSRGNDPIEFHNDWNDLPDNPNNAGTPGYTGDGIWSNDFFGGDLKGIDDKLDYLKGLGVSVIYLNPIFESPSNHKYDTADYTKIDEMFGTTQDFEKLMSDAHAKGINIILDGVFNHTSDDSIYFNRYGKYPDLGAYQDWKDGNQSLSPYGDWYTINSDGTYECWWGYDSLPVIKSLNGSEYNVTSWANFIINDKNAISKYWLNPDENLNDGADGWRLDVENEVAHDFWTHFRDAINTVKPEAPMIAENWGDASLDLLGDSFNSVMNYQFRNDIIDFLIGQSFDDGNGQHNPIDAAKLDQRLMSIYERYPLPAFYSTMNLLGSHDTMSILTVFGYNSADPNENSDAAKRLAEQKLKLATILQMGYPGMADIYYGDEAGVSGGKDPDDRRTFPWGNEDTALQDFFKNVSSIRNNNQVLKTGDLETLYAQNDVYAIGRRIINGKDAFGNSYPDSAAIVAINRSNSDQQITIDTTKFLRDGVAFKDLINGDKSYTINGGQITINIPAMSGVMLISDDGQDLTAPQVPSNVVATSGNGKVDLSWSQSDGATGYNIYRSSVEGGLYEKIASNVTGTTFEDTNVTNGLKYVYAISAVDELGNESEMSIDTVAYPAYPIGWVGNLTQVVDNHVISVSNPTEDIYAEVWADGLTNSTGQGPNMIAQLGYKYVGGTVNDSVYGSVYNSVYGVDDSDFTWVNAQYVGDIGNNDQYKASLHLINRSMGYLMRFSDNQGQSWTTTDTLSFYVVPSDDLIKPTAPILNQPGVESSRVSLTWSPSTDNVGIYNYEIYRSDGGTFNKIATVSNEVYNYVDTSVINGTTYSYKVVAADPSFNRTESNVVTIKPDVVPIKVTFNVTVPDYTPNSVNLAGTFPNATW |
| Enzyme Length | 1279 |
| Uniprot Accession Number | P36905 |
| 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 527; /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 (2); Metal binding (10); Region (1); Sequence caution (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..35; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 142,431 |
| Kinetics | |
| Metal Binding | METAL 248; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 250; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 288; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 343; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 401; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 403; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 406; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 407; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 452; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 454; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053 |
| Rhea ID | |
| Cross Reference Brenda |