Reviewed,
UniProtKB/Swiss-Prot P29767 (NANH_CLOSE)
Last modified
November 25, 2008.
Version 56.
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 |
| Organism | Clostridium septicum |
| Taxonomic identifier | 1504 [NCBI] |
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 1014 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
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. Contains 1 F5/8 type C domain. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell adhesionInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | exo-alpha-sialidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Potential | ||||||
| Chain | 27 – 1014 | 988 | Sialidase | PRO_0000012031 | |||||
Regions | |||||||||
| Domain | 39 – 186 | 148 | F5/8 type C | ||||||
| Repeat | 431 – 442 | 12 | BNR 1 | ||||||
| Repeat | 563 – 574 | 12 | BNR 2 | ||||||
| Repeat | 627 – 638 | 12 | BNR 3 | ||||||
| Repeat | 700 – 711 | 12 | BNR 4 | ||||||
Sites | |||||||||
| Active site | 421 | 1 | Proton acceptor By similarity | ||||||
| Active site | 912 | 1 | Nucleophile By similarity | ||||||
| Binding site | 396 | 1 | Substrate By similarity | ||||||
| Binding site | 688 | 1 | Substrate By similarity | ||||||
| Binding site | 873 | 1 | Substrate Potential | ||||||
Sequences
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References
| [1] | "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins." Rothe B., Rothe B., Roggentin P., Schauer R. Mol. Gen. Genet. 226:190-197(1991) [PubMed: 2034213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NC 0054714. |
Cross-references
Sequence databases | |
|---|---|
| X63266 Genomic DNA. Translation: CAA44916.1. | |
| PIR | NMCLSS. S15994. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SLL based on UniProtKB Q27701. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002860. BNR. IPR000421. Coagulation_factor_5/8-type_C. IPR013320. ConA_like_subgrp. IPR011490. FIVAR_sugar_bd. IPR004124. Glyco_hydro_33_N. [Graphical view] |
| Gene3D | G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. |
| Pfam | PF02012. BNR. 4 hits. PF00754. F5_F8_type_C. 1 hit. PF07554. FIVAR. 1 hit. PF02973. Sialidase. 1 hit. [Graphical view] |
| PROSITE | PS50022. FA58C_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NANH_CLOSE | ||||||||
| Accession | Primary (citable) accession number: P29767 | ||||||||
| 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


