| IED ID | IndEnz0001000387 |
| Enzyme Type ID | amylase000387 |
| Protein Name |
Neopullulanase SusA EC 3.2.1.135 Starch-utilization system protein A |
| Gene Name | susA BT_3704 |
| 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 | MKRNLLFIILLLLLPGLHQVFATSTIKKVAPTFWWAGMKNPELQILLYGDRISSADVSLSADNITLQEVVKQENPNYLVLYLDLSKAAPQNFDIILKQGKKQTKIPYELKQRRPNASAVEGFDSSDVLYLIMPDRFANGNPSNDIIPGMLEGNVDRNEPFARHGGDLKGIENHLDYIADLGVTSIWLNPIQENDMKEGSYHGYAITDYYQVDRRFGSNEEFRKLTQEANAKGLKVVMDMIFNHCGSDNYLFKDMPSKDWFNFEGNYVQTSFKTATQMDPYASDYEKKIAIDGWFTLTMPDFNQRNRHVATYLIQSSIWWIEYAGINGIRQDTHPYADFDMMARWCKAVNEEYPKFNIVGETWLGNNVLISYWQKDSRLAYPKNSNLPTVMDFPLMEEMNKAFDEETTEWNGGLFRLYEYLSQDIVYSHPMSLLTFLDNHDTSRFYRSEADTKNLDRYKQALTFLLTTRGIPQIYYGTEILMAADKANGDGLLRCDFPGGWPNDTKNCFDAANRTPQQNEAFSFMQKLLQWRKGNEVIAKGQLKHFAPNKGVYVYERKYGDKSVVVFLNGNDREQTIDLVPYQEILPASSAFDLLTEKKVELRNELTLPSREIYLLSF |
| Enzyme Length | 617 |
| Uniprot Accession Number | Q8A1G0 |
| Absorption | |
| Active Site | ACT_SITE 331; /evidence=ECO:0000250; ACT_SITE 360; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).; EC=3.2.1.135; |
| DNA Binding | |
| EC Number | 3.2.1.135 |
| Enzyme Function | FUNCTION: Neopullulanase that cleaves 1,4-alpha-glucosidic linkages in starch to produce disaccharides or trisaccharides in starch degradation. {ECO:0000269|PubMed:8955399}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; starch degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Frameshift (1); Metal binding (5); Sequence conflict (3); Signal peptide (1); Site (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Periplasm;Polysaccharide degradation;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8955399}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,184 |
| Kinetics | |
| Metal Binding | METAL 138; /note=Calcium; /evidence=ECO:0000250; METAL 143; /note=Calcium; /evidence=ECO:0000250; METAL 144; /note=Calcium; /evidence=ECO:0000250; METAL 164; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 166; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |