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P85512 (NAHA1_PALCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-hexosaminidase

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
NAHA1
OrganismPalythoa caribaeorum
Taxonomic identifier134933 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaHexacoralliaZoanthariaSphenopidaePalythoa

Protein attributes

Sequence length32 AA.
Sequence statusFragment.
Protein existenceEvidence 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 functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›32›32Beta-hexosaminidase
PRO_0000341515

Sites

Active site211Proton donor By similarity UniProtKB P23472

Experimental info

Non-terminal residue11
Non-terminal residue321

Sequences

Sequence LengthMass (Da)Tools
P85512 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 03DCDDB1A6FBC6F6

FASTA323,557
        10         20         30 
GKSSSRPLGD ATLGDLDFDI EVTQDYWDDL AR 

« Hide

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

3D structure databases

ProteinModelPortalP85512.
SMRP85512. Positions 1-32.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameNAHA1_PALCA
AccessionPrimary (citable) accession number: P85512
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries