Reviewed,
UniProtKB/Swiss-Prot P10481 (NANH_CLOPE)
Last modified
June 16, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Sialidase EC=3.2.1.18 Alternative name(s): Neuraminidase | ||
| Gene names |
| ||
| Organism | Clostridium perfringens | ||
| Taxonomic identifier | 1502 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 382 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Sialidases have been suggested to be pathogenic factors in microbial infections. |
| Catalytic activity | Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 33 family. Contains 4 BNR repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Repeat |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | exo-alpha-sialidase activity Inferred 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 – 382 | 382 | Sialidase | PRO_0000208908 | |||||
Regions | |||||||||
| Repeat | 71 – 82 | 12 | BNR 1 | ||||||
| Repeat | 140 – 151 | 12 | BNR 2 | ||||||
| Repeat | 208 – 219 | 12 | BNR 3 | ||||||
| Repeat | 255 – 266 | 12 | BNR 4 | ||||||
Sites | |||||||||
| Active site | 62 | 1 | Proton acceptor By similarity | ||||||
| Active site | 347 | 1 | Nucleophile By similarity | ||||||
| Binding site | 37 | 1 | Substrate By similarity | ||||||
| Binding site | 245 | 1 | Substrate Potential | ||||||
Sequences
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References
| [1] | "Cloning and sequencing of a Clostridium perfringens sialidase gene." Roggentin P., Rothe B., Lottspeich F., Schauer R. FEBS Lett. 238:31-34(1988) [PubMed: 2901987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 8-27. Strain: A99. |
Cross-references
Sequence databases | |
|---|---|
| Y00963 Genomic DNA. Translation: CAA68780.1. | |
| PIR | S01339. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2SIL based on UniProtKB P29768. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH33. Glycoside Hydrolase Family 33. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.18. 2406. |
Family and domain databases | |
| InterPro | IPR008377. Sialidase_trypan. [Graphical view] |
| PRINTS | PR01803. TCSIALIDASE. |
| ProtoNet | Search... |
Entry information
| Entry name | NANH_CLOPE | ||||||||
| Accession | Primary (citable) accession number: P10481 | ||||||||
| 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
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


