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P85512

- NAHA1_PALCA

UniProt

P85512 - NAHA1_PALCA

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Protein
Beta-hexosaminidase
Gene
N/A
Organism
Palythoa caribaeorum
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Preferentially hydrolyzes pNP-GlcNAc, hydrolyzes pNP-GalNAc to a lesser extent.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Enzyme regulationi

Activity is decreased by HgCl2 and maltose. Activity is stimulated by Na2SeO4, BaCl2, MgCl2, chondroitin 6-sulfate and phenylmethylsulfonyl fluoride.1 Publication

Kineticsi

  1. KM=0.53 mM for pNP-GlcNAc1 Publication

Vmax=88.1 µmol/h/mg enzyme with pNP-Glc-NAc as substrate1 Publication

pH dependencei

Optimum pH is 5.0. Active over a broad range of pH values.1 Publication

Temperature dependencei

Has maximum activity at 45 to 60 degrees Celsius. Inactive at temperatures of 70 degrees Celsius and above.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei21 – 211Proton donor By similarityBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase (EC:3.2.1.52)
    Alternative name(s):
    Beta-N-acetylhexosaminidase
    N-acetyl-beta-glucosaminidase
    NAHA1
    OrganismiPalythoa caribaeorum
    Taxonomic identifieri134933 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaZoanthariaSphenopidaePalythoa

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›32›32Beta-hexosaminidase
    PRO_0000341515Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP85512.
    SMRiP85512. Positions 1-32.

    Family & Domainsi

    Sequence similaritiesi

    Sequencei

    Sequence statusi: Fragment.

    P85512-1 [UniParc]FASTAAdd to Basket

    « Hide

    GKSSSRPLGD ATLGDLDFDI EVTQDYWDDL AR                      32
    Length:32
    Mass (Da):3,557
    Last modified:June 10, 2008 - v1
    Checksum:i03DCDDB1A6FBC6F6
    GO

    Non-terminal residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei32 – 321

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P85512.
    SMRi P85512. Positions 1-32.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiNAHA1_PALCA
    AccessioniPrimary (citable) accession number: P85512
    Entry historyi
    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 statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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