ID   NAHA1_PALCA             Reviewed;          32 AA.
AC   P85512;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   AltName: Full=NAHA1;
DE   Flags: Fragment;
OS   Palythoa caribaeorum (White encrusting zoanthid coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Zoantharia;
OC   Sphenopidae; Palythoa.
OX   NCBI_TaxID=134933;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18171621; DOI=10.1016/j.pep.2007.10.024;
RA   Souza D.S.L., Grossi-de-Sa M.F., Silva L.P., Franco O.L.,
RA   Gomes-Junior J.E., Oliveira G.R., Rocha T.L., Magalhaes C.P., Marra B.M.,
RA   Grossi-de-Sa M., Romano E., de Sa C.M., Kombrink E., Jimenez A.V.,
RA   Abreu L.R.D.;
RT   "Identification of a novel beta-N-acetylhexosaminidase (Pcb-NAHA1) from
RT   marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea).";
RL   Protein Expr. Purif. 58:61-69(2008).
CC   -!- FUNCTION: Preferentially hydrolyzes pNP-GlcNAc, hydrolyzes pNP-GalNAc
CC       to a lesser extent. {ECO:0000269|PubMed:18171621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000269|PubMed:18171621};
CC   -!- ACTIVITY REGULATION: Activity is decreased by HgCl(2) and maltose.
CC       Activity is stimulated by Na(2)SeO(4), BaCl(2), MgCl(2), chondroitin 6-
CC       sulfate and phenylmethylsulfonyl fluoride.
CC       {ECO:0000269|PubMed:18171621}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.53 mM for pNP-GlcNAc {ECO:0000269|PubMed:18171621};
CC         Vmax=88.1 umol/h/mg enzyme with pNP-Glc-NAc as substrate
CC         {ECO:0000269|PubMed:18171621};
CC       pH dependence:
CC         Optimum pH is 5.0. Active over a broad range of pH values.
CC         {ECO:0000269|PubMed:18171621};
CC       Temperature dependence:
CC         Has maximum activity at 45 to 60 degrees Celsius. Inactive at
CC         temperatures of 70 degrees Celsius and above.
CC         {ECO:0000269|PubMed:18171621};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85512; -.
DR   SMR; P85512; -.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase.
FT   CHAIN           <1..>32
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000341515"
FT   DOMAIN          <1..>32
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        21
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18171621"
FT   NON_TER         32
FT                   /evidence="ECO:0000303|PubMed:18171621"
SQ   SEQUENCE   32 AA;  3557 MW;  03DCDDB1A6FBC6F6 CRC64;
     GKSSSRPLGD ATLGDLDFDI EVTQDYWDDL AR