ID   HEX20_CELFI             Reviewed;         496 AA.
AC   Q7WUL4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Beta-N-acetylhexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylgalactosaminidase;
DE   AltName: Full=Beta-N-acetylglucosaminidase;
DE   AltName: Full=Hex20;
GN   Name=hex20; Synonyms=hex20A;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16762038; DOI=10.1111/j.1742-4658.2006.05308.x;
RA   Mayer C., Vocadlo D.J., Mah M., Rupitz K., Stoll D., Warren R.A.J.,
RA   Withers S.G.;
RT   "Characterization of a beta-N-acetylhexosaminidase and a beta-N-
RT   acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi.";
RL   FEBS J. 273:2929-2941(2006).
CC   -!- FUNCTION: Catalyzes the cleavage of beta-N-acetylglucosaminides and
CC       beta-N-acetylgalactosaminides. Also catalyzes the hydrolysis of N-
CC       acetylchitooligomers. May be involved in chitin degradation. It is not
CC       able to cleave beta-glucosides. {ECO:0000269|PubMed:16762038}.
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:16762038};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=53 uM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide
CC         {ECO:0000269|PubMed:16762038};
CC         KM=66 uM for 4'-nitrophenyl beta-N-acetyl-D-galactosaminide
CC         {ECO:0000269|PubMed:16762038};
CC         Note=There is a 4-fold greater activity on 4'-nitrophenyl beta-N-
CC         acetyl-D-glucosaminide than on 4'-nitrophenyl beta-N-acetyl-D-
CC         galactosaminide.;
CC       pH dependence:
CC         Optimum pH is 7.3-8.7 with 4'-nitrophenyl beta-N-acetyl-D-
CC         glucosaminide as substrate. Rapidly inactivated above pH 9.5 and
CC         stable from pH 6.0 to 9.5. {ECO:0000269|PubMed:16762038};
CC   -!- PATHWAY: Glycan degradation; chitin degradation.
CC   -!- MISCELLANEOUS: The reaction mechanism involves an oxazolinium ion
CC       intermediate.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; AF478459; AAQ05800.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7WUL4; -.
DR   SMR; Q7WUL4; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   SABIO-RK; Q7WUL4; -.
DR   UniPathway; UPA00349; -.
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:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.379.10; -; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR22600; PTHR22600; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation.
FT   CHAIN           1..496
FT                   /note="Beta-N-acetylhexosaminidase"
FT                   /id="PRO_0000252455"
FT   ACT_SITE        298
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  53326 MW;  7D514C614991706C CRC64;
     MPDVAVIPRP VLLETTDGPP FVLTAATILV VDSAPELVAV GVLAADLLGR LSGRPVEVRY
     TEGGAPSVVR LRLSEDLPAG DEAYRLVVSE HRVDIDARSA AGLVRAVVTL RQTVSSLGDG
     TLTVPALRVE DHPRYAWRGL SIDVARHFFT VDDLKAIIGL LAHYKLNVLH LHLTDDQGWR
     VHLPSRPHLT RASAGTSVGG GPGGFYNPAQ LAEIVVARAA RGIRVVPEID VPGHVNAATH
     AYGDLTPSGE PTDVYTGIEV GFSRLHDDLP ATRPFLRDVF TDLAAMTPGE YVHIGGDEVL
     TMDHDKYARL VGYAASVVRD AGKKVVGWQE ISSTPLEPGT VVQYWDINAD PAPFVAAAQA
     GAHVLMSPGS RAYLDMKYDA TTELGLEWAG HIELRDAYDW EPSTLIPGVP PESVIGVEAA
     VWTETLTDLG ELTSMLLPRL AAVAEVAWTA PQDRDWDDFS GRVAQHAPFW DRVGFRWHAS
     PQVSWPGPGS APGAAF