| IED ID | IndEnz0001000409 |
| Enzyme Type ID | amylase000409 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 |
| Gene Name | igtZ |
| Organism | Niallia circulans (Bacillus circulans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Niallia Niallia circulans (Bacillus circulans) |
| Enzyme Sequence | MTRKTRYLHQITTLILGGLLIVPAAAPPVSADIAATHVYHNHMPNFWAYYDLNTYNSTPVGSPIRYTYDGEVIQLKQNPPAGYPYYLPNGSPMPHDDLVSYYSHHAKTGAYLTWPWSVANTLHSSHPQAQMHVTMSGSVVNNVNSIIQQGNVSGYNNPAWGTPWKNAVTQLKTAGGDNRLDLIHFSGHHSMGPLVGNDYLLKDMIYHGATMAQPYFLGSSYKSSKGFFPTELGFSERIIPVLNKLGIQWSVIGNNHFSRTLKDYPLLDSPGTDTMISPPNRSDLQNVSTAGAWVNEPMFNEQQVVYNKYPFASTAHWVRYVDPATGAESRVVGVPVAQAQSWEEGYLGQVKADALKPYENLVAQKQIFVVAHDGDNSSGRAGSEETWRNAGNVTYADSGVTGMGIDEYLRSNTPAAADVVHVQDGSWIDTRDSSSDPAWYHWHLPFGIWKGQFAAFNQVNGTAYAPKKNLAGVEEGMTVSFEKGYHYLERNFALLQASLNYAKTAEQIWLEEHPNYWKPANPLDREVTYEGNQLNPWMLSYPVKGNPANDYAGGANPAELAWYFLLPAMDSGFGYYDENVDDSVKPALSFNQSLYFSKPYVSQKLAKDKTGPSVWWPQRYPYNPGSANVSKAEGWTLQHYNNAFAIYTYAFDTSGISEIKVKVRAHRDKTADAADNTFKVYDPAGLAAAGIANIDPAKVGAWTEYPMNVRDLSADINGVDWQPSSMTIMQKVPATDIGNLYFSYISDYRDQLLDYFIEAKDAKGNVTQSDIQQVYVGAGKYKLANGKYTESMQGTIEGTHPFITDVPAVPDTEAPAVPANLQATVMNASSVGLSWNAATDNIRVTGYEIYRNGVRIGTTPSTSYTDSGLSASTAYEYRVKAYDASGNLSGFSAAATATTPAGNHVTVYYKQGYSTPYIHYRPAGGTWTTAPGVAIPAAEVAGYNKITINIGAATQLEACFNNGSGTWDSNGGSNYLFGTGTWTYTPTGKIQAGAPVAPSATPTVAPTATPTPKPSVTPTVTPITTPTVAPTLSPTPTVAPTVKPSATPIATPTVTPTVSPTATPTVVPTIAPTATPTTSPSATPVPTATPAGNSATIYYKNTAFSNSYIHYKLDGATAWTTSPGVQMQASTFSGYKAITIPLGSATGLTAAFNNGSGIWDNNGGSNYHFGTGSSSLTGGNLITGEPQADSVTFRVSVPGSTPANAPVYLTGSFNSWNAADPAYLLTRGSDGIYSITLNLPAGSAVTYKLTRGSWATVETASSGADITNRTLTPAGGAQTVTLTVQRWKDQ |
| Enzyme Length | 1290 |
| Uniprot Accession Number | A0P8X0 |
| Absorption | |
| Active Site | ACT_SITE 231; /note=Nucleophile; /evidence=ECO:0000305|PubMed:22819817; ACT_SITE 373; /note=Proton donor; /evidence=ECO:0000305|PubMed:22819817 |
| Activity Regulation | |
| Binding Site | |
| 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; Evidence={ECO:0000269|PubMed:17090949}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Acts on maltooligosaccharides that have a degree of polymerization (DP) of 4 or more, amylose, and soluble or raw starch to produce glucose and maltooligosaccharides up to DP5 by a hydrolysis reaction. Also acts on maltooligosyl trehaloses that have DP5 or more to produce trehalose as the major hydrolysis product. {ECO:0000269|PubMed:17090949}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:17090949}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:17090949}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (2); Region (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:17090949 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 138,787 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |