| IED ID | IndEnz0001000336 |
| Enzyme Type ID | amylase000336 |
| Protein Name |
Pullulanase A EC 3.2.1.41 Alpha-dextrin endo-1,6-alpha-glucosidase Pullulan 6-glucanohydrolase |
| Gene Name | spuA |
| Organism | Streptococcus pneumoniae |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae |
| Enzyme Sequence | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPATEPTTPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQIFLKDDDESIYTNPYYVHDIRMTGAQHVGTSSIESSFSTLVGAKKEDILKHSNITNHLGNKVTITDVAIDEAGKKVTYSGDFSDTKHPYTVSYNSDQFTTKTSWRLKDETYSYDGKLGADLKEEGKQVDLTLWSPSADKVSVVVYDKNDPDKVVGTVALEKGERGTWKQTLDSTNKLGITDFTGYYYQYQIERQGKTVLALDPYAKSLAAWNSDDAKIDDAHKVAKAAFVDPAKLGPQDLTYGKIHNFKTREDAVIYEAHVRDFTSDPAIAKDLTKPFGTFEAFIEKLDYLKDLGVTHIQLLPVLSYYFVNELKNHEHLSDYASSNSNYNWGYDPQNYFSLTGMYSSDPKNPEKRIAEFKNLINEIHKRGMGAILDVVYNHTAKVDIFEDLEPNYYHFMDADGTPRTSFGGGRLGTTHHMTKRLLVDSIKYLVDTYKVDGFRFDMMGDHDAASIEEAYKAARALNPNLIMLGEGWRTYAGDENMPTKAADQDWMKHTDTVAVFSDDIRNNLKSGYPNEGQPAFITGGKRDVNTIFKNLIAQPTNFEADSPGDVIQYIAAHDNLTLFDIIAQSIKKDPSKAENYAEIHRRLRLGNLMVLTAQGTPFIHSGQEYGRTKQFRNPAYRTPVAEDKVPNKSHLLRDKDGNPFDYPYFIHDSYDSSDAVNKFDWTKATDGKAYPENVKSRDYMKGLIALRQSTDAFRLKSLQDIKDRVHLITVPGQNGVEKEDVVIGYQITAPNGDIYAVFVNADEKAREFNLGTAFAHLRNAEVLADENQAGSVGIANPKGLEWTEKGLKLNALTATVLRVSQNGTSHESTAEEKPDSTPSKPEHQNEASHPAHQDPAPEARPDSTKPDAKVADAENKPSQATADSQAEQPAQEAQASSVKEAVRKESVENSSKENISATPDRQAELPNTGIKNENKLLFAGISLLALLGLGFLLKNKKEN |
| Enzyme Length | 1287 |
| Uniprot Accession Number | Q9F930 |
| Absorption | |
| Active Site | ACT_SITE 785; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; ACT_SITE 814; /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 175; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 221; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 283; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 325; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 330; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 750; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 816; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 846; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 849; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 856; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 903; /note=Substrate; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; BINDING 976; /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:0000269|PubMed:11083842}; |
| DNA Binding | |
| EC Number | 3.2.1.41 |
| Enzyme Function | FUNCTION: Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen (By similarity). Hydrolyzes pullulan (PubMed:11083842). 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:0000250|UniProtKB:A0A0H2ZL64, ECO:0000269|PubMed:11083842}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (12); Chain (1); Compositional bias (5); 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:0000269|PubMed:11083842}. 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 1256; /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 1253..1257; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 143,317 |
| Kinetics | |
| Metal Binding | METAL 668; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 670; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 835; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 838; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 839; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 889; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 893; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0; METAL 999; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:A0A0H2UNG0 |
| Rhea ID | |
| Cross Reference Brenda |