| IED ID | IndEnz0001000025 |
| Enzyme Type ID | amylase000025 |
| Protein Name |
Alpha-amylase MalA EC 3.2.1.1 |
| Gene Name | malA C444_04352 |
| Organism | Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Halobacteriales Haloarculaceae Haloarcula Haloarcula japonica Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) |
| Enzyme Sequence | MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ |
| Enzyme Length | 663 |
| Uniprot Accession Number | L8B068 |
| Absorption | |
| Active Site | ACT_SITE 411; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q08751; ACT_SITE 440; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q08751 |
| Activity Regulation | ACTIVITY REGULATION: Stable and active over a broad range of NaCl concentrations (0.5 to 4.2 M NaCl), with maximal activity at 2.6 M NaCl. 83% and 94% of the maximum activity at 0.6 and 4.2 M NaCl, respectively. Active and stable also in KCl. {ECO:0000269|PubMed:23391916}. |
| 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:23391916}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alpha-1,6 bonds. Higher activities of 100%, 79% and 67.8% against amylose, soluble starch and amylopectin, respectively. Lower activity of 22% against glycogen and faint or no activity against alpha-, beta- and gamma-cyclodextrin. {ECO:0000250|UniProtKB:Q8A1G3, ECO:0000269|PubMed:23391916}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius in 2.0 M NaCl and at pH 6.5. Relatively stable up to 55 degrees Celsius. {ECO:0000269|PubMed:23391916}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 in 2.0 M NaCl. Stable over a range of pH 5.7-9.2. {ECO:0000269|PubMed:23391916}; |
| Pathway | PATHWAY: Glycan degradation; starch degradation. {ECO:0000250|UniProtKB:Q8A1G3}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Region (2); Site (1) |
| Keywords | Carbohydrate metabolism;Cytoplasm;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23391916}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 72,027 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |