| IED ID | IndEnz0001000338 |
| Enzyme Type ID | amylase000338 |
| Protein Name |
Alpha-amylase SusG EC 3.2.1.1 Starch-utilization system protein G |
| Gene Name | susG BT_3698 |
| Organism | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Bacteroidaceae Bacteroides Bacteroides thetaiotaomicron Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
| Enzyme Sequence | MNKHLHFLSLLWLSMLMAFMTACSDDKNITDPAPEPEPPVEGQWTALTASPDTWDETKRADISYQLLLYSFADSDGDGYGDLNGVTQKLDYLNQLGVKALWLSPIHPCMSYHGYDVTDYTKVNPQLGTESDFDRLVTEAHNRGIKIYLDYVMNHTGTAHPWFTEASSSSESPYRNYYSFSEDPKTDIAAGKIAMITQEGAAGYNAAEWFQVSDETAAVKGLLKFTLDWSNAPSPILVVSTGTKADEDNPDTGTDNAKYLYYGEDICKKFYDKGNNIYELTVDFESTWGLLIRTSNASFWPSGTKYGASSSSEKLALNKDFKLTNAGNPANIMFDSQQITYFHSHFCTDWFADLNYGPVDQAGESPAYQAIADAAKGWIARGVDGLRLDAVKHIYHSETSEENPRFLKMFYEDMNAYYKQKGHTDDFYMIGEVLSEYDKVAPYYKGLPALFEFSFWYRLEWGINNSTGCYFAKDILSYQQKYANYRSDYIEATKLSNHDEDRTSSKLGKSADKCKLAAAVLLTSAGHPYIYYGEELGLYGTKDNGDEYVRSPMLWGDSYTTNYTDKTDATVSKNVKTVADQQADTHSLLNIYFSLTRLRNTYPALAEGNMTKHSVYNESQEKDYKPIAAWYMTKDNEKLLVIHNFGGTAMQLPLTDKIEKVLFVNGETQQNTDSDSYTLKLGGYASVVFKLGN |
| Enzyme Length | 692 |
| Uniprot Accession Number | Q8A1G3 |
| Absorption | |
| Active Site | ACT_SITE 388; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 431; /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; Evidence={ECO:0000269|PubMed:20159465}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Alpha-amylase that cleaves starch into oligosaccharides before internalization for degradation, the first step in starch degradation. {ECO:0000269|PubMed:10572122, ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:20159465}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; starch degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (39); Chain (1); Helix (28); Lipidation (2); Metal binding (8); Mutagenesis (4); Region (6); Sequence conflict (5); Signal peptide (1); Site (5); Turn (6) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cell outer membrane;Glycosidase;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Palmitate;Polysaccharide degradation;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: By maltose. {ECO:0000269|PubMed:9006015}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:10572122}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:10572122}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3K8K; 3K8L; 3K8M; 6BS6; |
| Mapped Pubmed ID | 29603462; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,959 |
| Kinetics | |
| Metal Binding | METAL 73; /note=Magnesium; /evidence=ECO:0000269|PubMed:20159465; METAL 75; /note=Magnesium; /evidence=ECO:0000269|PubMed:20159465; METAL 77; /note=Magnesium; /evidence=ECO:0000269|PubMed:20159465; METAL 79; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20159465; METAL 81; /note=Magnesium; /evidence=ECO:0000269|PubMed:20159465; METAL 153; /note=Calcium; /evidence=ECO:0000269|PubMed:20159465; METAL 352; /note=Calcium; /evidence=ECO:0000269|PubMed:20159465; METAL 392; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:20159465 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |