Reviewed,
UniProtKB/Swiss-Prot C0SPA0 (PULA_BACSU)
Last modified
November 24, 2009.
Version 8.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pullulanase EC=3.2.1.41 Alternative name(s): Alpha-dextrin endo-1,6-alpha-glucosidase Pullulan 6-glucanohydrolase | ||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 718 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 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. |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. |
| Biophysicochemical properties | Kinetic parameters: Vmax=27.6 µmol/min/mg enzyme (at pH 5.4) pH dependence: Optimum pH is 6.0. Temperature dependence: Optimum temperature is 40 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosidase Hydrolase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro pullulanase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 718 | 718 | Pullulanase | PRO_0000381992 | |||||
Sites | |||||||||
| Active site | 406 | 1 | Nucleophile By similarity | ||||||
| Active site | 435 | 1 | Proton donor By similarity | ||||||
| Active site | 525 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 553 | 1 | A → V in AAC00283. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION. |
| [4] | "Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168." Malle D., Itoh T., Hashimoto W., Murata K., Utsumi S., Mikami B. Acta Crystallogr. F 62:381-384(2006) [PubMed: 16582490] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 168. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF008220 Genomic DNA. Translation: AAC00283.1. AL009126 Genomic DNA. Translation: CAB14971.2. | |||||||||||||||||||||||||
| PIR | G69585. | ||||||||||||||||||||||||
| RefSeq | NP_390871.2. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| CAZy | CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 937292. | ||||||||||||||||||||||||
| GenomeReviews | Gene locus BSU29930 in contig AL009126_GR. | ||||||||||||||||||||||||
| NMPDR | fig|224308.1.peg.2996. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| SubtiList | BG12566. amyX. [Micado] | ||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR006047. Glyco_hydro_13_cat. IPR004193. Glyco_hydro_13_N. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. IPR011840. PulA_typeI. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00128. Alpha-amylase. 1 hit. PF02922. CBM_48. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| TIGRFAMs | TIGR02104. pulA_typeI. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | PULA_BACSU | ||||||||
| Accession | Primary (citable) accession number: C0SPA0 Secondary accession number(s): O34587, Q795S6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


