ID   HEXA_PSEO7              Reviewed;         598 AA.
AC   P48823;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Beta-hexosaminidase A;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=Chitobiase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   Flags: Precursor;
GN   Name=cht60;
OS   Pseudoalteromonas piscicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 12-22.
RC   STRAIN=O-7;
RX   PubMed=8063094; DOI=10.1016/0378-1119(94)90843-5;
RA   Tsujibo H., Fujimoto K., Tanno H., Miyamoto K., Imada C., Okami Y.,
RA   Inamori Y.;
RT   "Gene sequence, purification and characterization of N-acetyl-beta-
RT   glucosaminidase from a marine bacterium, Alteromonas sp. strain O-7.";
RL   Gene 146:111-115(1994).
CC   -!- FUNCTION: Most active towards p-nitrophenyl-N-acetyl-beta-D-
CC       glucosaminide(PNP-beta-GlcNAc) and diacetylchitobiose.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; D17399; BAA04223.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48823; -.
DR   SMR; P48823; -.
DR   STRING; 43662.TW75_07800; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
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   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..11
FT                   /evidence="ECO:0000269|PubMed:8063094"
FT   CHAIN           12..598
FT                   /note="Beta-hexosaminidase A"
FT                   /id="PRO_0000011784"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   598 AA;  64539 MW;  5131B17B84DA9688 CRC64;
     MSFITSAHAT AAQVPLTTSQ MLGQKLMLDF RYYCGESKKP SGDCRAAMTT LPPELSELIS
     RYDIGGAILF AENVQNTAQI ISLTNALQSA AQQSKSQLPL FIAIDQEGGR VARINREQAT
     SFTGNMSIGA TYPKQGDIYA TKVASAIGKE LNSLGINVNF APTVDVNSNP NNPVINVRSF
     SENPTVVTKL GLAQVKAFEA AGVLSALKHF PGHGDTHVDS HTGLPRVDHD RDKINQQDLL
     PFAEIIKASP PGMIMTAHIQ YPALDNSKVV NSQGESMIRP ATMSYQIMTQ LLRHELGYQG
     VTVTDALDMA GISDFFNPVD ATIETFNAGV DIALMPIAIR NRADIKRFEQ YMAQLADALE
     TNKLNQEQLS SSMARIAKLK TKLPQSSASL AIANSTLGNP SHRRLEAELA LAAITEVKND
     GVLPLRDNAQ VVHLIMPDRQ KCFALEQALQ TYSKNSLTLS CTSLQAYDPD IAHDAIKQAD
     MIIAAHASPP QSAVEIGGMD DVKKLREHGV ARNVQPAALK ALLQYGQQQG KKQLFISLRA
     PYEISTFGPL SNAVLASYAY NVDVNHDKKV AGPAYTALAK VILGIAKAEG SLPVTVNH