| IED ID | IndEnz0001000349 |
| Enzyme Type ID | amylase000349 |
| Protein Name |
Pullulanase A EC 3.2.1.41 Alpha-dextrin endo-1,6-alpha-glucosidase Pullulan 6-glucanohydrolase |
| Gene Name | spuA SPD_0250 |
| Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
| Enzyme Sequence | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAADSGKNESDISSPRNANASLEKTEEKPATEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWHLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDAKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHERLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDIFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLVDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRDPAYKTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGSVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVQNESVENSSKKNIPATPDRQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN |
| Enzyme Length | 1256 |
| Uniprot Accession Number | A0A0H2ZL64 |
| Absorption | |
| Active Site | ACT_SITE 763; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; ACT_SITE 792; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 4-O-alpha-D-glucopyranosylmoranoline (G1M). {ECO:0000250|UniProtKB:A0A0H2UNG0}. |
| Binding Site | BINDING 153; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 199; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 261; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 303; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 308; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 728; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 794; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 824; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 827; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 834; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 881; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 954; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41; Evidence={ECO:0000250|UniProtKB:A0A0H2UNG0}; |
| DNA Binding | |
| EC Number | 3.2.1.41 |
| Enzyme Function | FUNCTION: Virulence factor (PubMed:17041037). Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not hydrolyze dextran. Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose) (By similarity). {ECO:0000250|UniProtKB:A0A0H2UNG0, ECO:0000269|PubMed:17041037}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (12); Chain (1); Compositional bias (3); Metal binding (8); Modified residue (1); Motif (1); Propeptide (1); Region (6); Signal peptide (1); Site (1) |
| Keywords | Calcium;Cell wall;Glycosidase;Hydrolase;Metal-binding;Peptidoglycan-anchor;Secreted;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000250|UniProtKB:A0A0H2UNG0}. |
| Modified Residue | MOD_RES 1225; /note=Pentaglycyl murein peptidoglycan amidated threonine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..44; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 1222..1226; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 140,279 |
| Kinetics | |
| Metal Binding | METAL 646; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 648; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 813; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 816; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 817; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 867; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 871; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 977; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0 |
| Rhea ID | |
| Cross Reference Brenda |