ID   HEX_VIBVL               Reviewed;         847 AA.
AC   Q04786;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=Chitobiase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
GN   Name=hex;
OS   Vibrio vulnificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27562 / DSM 10143 / JCM 3725 / BCRC 12905 / KCTC 2959 / LMG
RC   13545 / NBRC 15645 / NCIMB 2046 / WDCM 00139;
RX   PubMed=8341694; DOI=10.1073/pnas.90.14.6751;
RA   Somerville C.C., Colwell R.R.;
RT   "Sequence analysis of the beta-N-acetylhexosaminidase gene of Vibrio
RT   vulnificus: evidence for a common evolutionary origin of hexosaminidases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6751-6755(1993).
CC   -!- FUNCTION: Hydrolysis of terminal, non-reducing N-acetyl-beta-D-
CC       glucosamine residues in chitobiose and higher analogs, and in
CC       glycoproteins.
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   -!- PATHWAY: Glycan degradation; chitin degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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   EMBL; L04544; AAA27527.1; -; Genomic_DNA.
DR   PIR; A48228; A48228.
DR   AlphaFoldDB; Q04786; -.
DR   SMR; Q04786; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PRIDE; Q04786; -.
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:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02847; E_set_Chitobiase_C; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.30.379.10; -; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004866; CHB/HEX_N_dom.
DR   InterPro; IPR004867; CHB_C_dom.
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   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22600; PTHR22600; 1.
DR   Pfam; PF03173; CHB_HEX; 1.
DR   Pfam; PF03174; CHB_HEX_C; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SMART; SM01081; CHB_HEX; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW   Hydrolase; Polysaccharide degradation.
FT   CHAIN           1..847
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000215378"
FT   ACT_SITE        519
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..40
FT                   /evidence="ECO:0000250"
FT   DISULFID        377..385
FT                   /evidence="ECO:0000250"
FT   DISULFID        484..530
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   847 AA;  94277 MW;  3C4405EFA34F3D14 CRC64;
     MASDIDQKDV DYAAKNLKLT TSLVANKPKD CPPEAPWGAC YRVEINLENT GSKSLNENVE
     IYFSSIHRTL GSKSEEFKVE HINGDLHKIT TTEKFKGLKG GKTKSFQVDF MNWIVSNSDF
     MPNYYVASEH LEGRNILNTV PIDAVHITEE VSGFTTGIKH TPNQLKRTAN DLLPAATATT
     RYEQYSKVKD LGADAVSAHI LPTPLETSVH EGSLNIAQGI NIVSDALPAD QVEALNFRFE
     TLGVNTGTGV PVNVTIKADS SKKSGSYTLD VTSSGIRIVG VDKAGAFYGV QSLAGLVTVG
     KDTINQVSIN DEPRLDYRGM HMDVSRNFHS KELVFRFLDQ MAAYKMNKFH FHLADDEGWR
     LEINGLPELT QVGAHRCHDV EQNKCMMPQL GSGAELPNNG SGYYTREDYK EILAYASARN
     IQVIPSMDMP GHSLAAVKSM EARYRKFMAE GDVVKAEMYL LSDPNDTTQY YSIQHYQDNT
     INPCMESSFV FMDKVIDEIN KLHKEGGQPL TDYHIGADET AGAWGDSPEC RKMFVAPESG
     VKNAKDINGY FINRISHILD AKGLTLGAWN DGLSHKALDA SSLAGNPPKA WVWGTMFWGG
     VDQYNSFANK GYDVVVTPPD AYYFDMPYEN DPEERGYYWA TRFNDTKKVF SFMPENVPAN
     VEWMTDRMGA KISATTGEKT HDFLGVQGAL WSETIRTDAQ VEYMVLPRMI AVAERGWHKA
     SWEEEHKEGI TYTSNVDGHE GTTHLNDNIA TRDADWAHFS NILGYKEMPK LDKAGITYRL
     PVLGAVIKNN ILDVVTEFHG VAIQYSLDGK TWHKYDDTKK PQVSTKALVR SVSTNGRTGR
     AVEVLAK