| IED ID | IndEnz0001000026 |
| Enzyme Type ID | amylase000026 |
| Protein Name |
Periplasmic alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | malS b3571 JW3543 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKLAACFLTLLPGFAVAASWTSPGFPAFSEQGTGTFVSHAQLPKGTRPLTLNFDQQCWQPADAIKLNQMLSLQPCSNTPPQWRLFRDGEYTLQIDTRSGTPTLMISIQNAAEPVASLVRECPKWDGLPLTVDVSATFPEGAAVRDYYSQQIAIVKNGQIMLQPAATSNGLLLLERAETDTSAPFDWHNATVYFVLTDRFENGDPSNDQSYGRHKDGMAEIGTFHGGDLRGLTNKLDYLQQLGVNALWISAPFEQIHGWVGGGTKGDFPHYAYHGYYTQDWTNLDANMGNEADLRTLVDSAHQRGIRILFDVVMNHTGYATLADMQEYQFGALYLSGDEVKKSLGERWSDWKPAAGQTWHSFNDYINFSDKTGWDKWWGKNWIRTDIGDYDNPGFDDLTMSLAFLPDIKTESTTASGLPVFYKNKMDTHAKAIDGYTPRDYLTHWLSQWVRDYGIDGFRVDTAKHVELPAWQQLKTEASAALREWKKANPDKALDDKPFWMTGEAWGHGVMQSDYYRHGFDAMINFDYQEQAAKAVDCLAQMDTTWQQMAEKLQGFNVLSYLSSHDTRLFREGGDKAAELLLLAPGAVQIFYGDESSRPFGPTGSDPLQGTRSDMNWQDVSGKSAASVAHWQKISQFRARHPAIGAGKQTTLLLKQGYGFVREHGDDKVLVVWAGQQ |
| Enzyme Length | 676 |
| Uniprot Accession Number | P25718 |
| Absorption | |
| Active Site | ACT_SITE 460; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 503; /note=Proton donor; /evidence=ECO:0000250 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through the cytoplasmic membrane via the membrane-bound complex of three proteins, MalF, MalG, and MalK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the MalS protein. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Metal binding (2); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Periplasm;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Under the regulatory control of the MalT protein. |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000269|PubMed:1544897 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15690043; |
| Motif | |
| Gene Encoded By | |
| Mass | 75,713 |
| Kinetics | |
| Metal Binding | METAL 314; /note=Calcium; /evidence=ECO:0000250; METAL 464; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |