P85512 (NAHA1_PALCA) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 16.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-hexosaminidase EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase N-acetyl-beta-glucosaminidase NAHA1 |
| Organism | Palythoa caribaeorum |
| Taxonomic identifier | 134933 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Cnidaria › Anthozoa › Hexacorallia › Zoanthidea › Sphenopidae › Palythoa![]() |
Protein attributes
| Sequence length | 32 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Preferentially hydrolyzes pNP-GlcNAc, hydrolyzes pNP-GalNAc to a lesser extent. Ref.1 |
| Catalytic activity | Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.1 |
| Enzyme regulation | Activity is decreased by HgCl2 and maltose. Activity is stimulated by Na2SeO4, BaCl2, MgCl2, chondroitin 6-sulfate and phenylmethylsulfonyl fluoride. Ref.1 |
| Sequence similarities | Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=0.53 mM for pNP-GlcNAc Ref.1 Vmax=88.1 µmol/h/mg enzyme with pNP-Glc-NAc as substrate Ref.1 pH dependence: Optimum pH is 5.0. Active over a broad range of pH values. Ref.1 Temperature dependence: Has maximum activity at 45 to 60 degrees Celsius. Inactive at temperatures of 70 degrees Celsius and above. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular_function | beta-N-acetylhexosaminidase 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 – ›32 | ›32 | Beta-hexosaminidase | PRO_0000341515 | |||||
Sites | |||||||||
| Active site | 21 | 1 | Proton donor By similarity UniProtKB P23472 | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 32 | 1 | |||||||
Sequences
References
| [1] | "Identification of a novel beta-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)." Souza D.S.L., Grossi-de-Sa M.F., Silva L.P., Franco O.L., Gomes-Junior J.E., Oliveira G.R., Rocha T.L., Magalhaes C.P., Marra B.M., Grossi-de-Sa M., Romano E., de Sa C.M., Kombrink E., Jimenez A.V., Abreu L.R.D. Protein Expr. Purif. 58:61-69(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. |
Cross-references
Entry information
| Entry name | NAHA1_PALCA | ||||||||
| Accession | Primary (citable) accession number: P85512 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
