ID   HEXB_ENTHI              Reviewed;         565 AA.
AC   Q86M34;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Beta-hexosaminidase subunit beta;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-GlcNAcase subunit beta;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit beta;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit beta;
DE   Flags: Precursor;
GN   Name=HEXB;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-33; 146-155 AND 307-316,
RP   FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND INTERACTION WITH HEXA.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=15555733; DOI=10.1016/j.molbiopara.2004.09.003;
RA   Riekenberg S., Flockenhaus B., Vahrmann A., Mueller M.C.M., Leippe M.,
RA   Kiess M., Scholze H.H.;
RT   "The beta-N-acetylhexosaminidase of Entamoeba histolytica is composed of
RT   two homologous chains and has been localized to cytoplasmic granules.";
RL   Mol. Biochem. Parasitol. 138:217-225(2004).
CC   -!- FUNCTION: Hexoaminidase complex may contribute to amoebic pathogenicity
CC       and may be involved in the destruction of extracellular matrix
CC       components. {ECO:0000269|PubMed:15555733}.
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   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC       {ECO:0000269|PubMed:15555733}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:15555733}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; AJ417748; CAD10500.3; -; Genomic_DNA.
DR   AlphaFoldDB; Q86M34; -.
DR   SMR; Q86M34; -.
DR   STRING; 5759.rna_EHI_007330-1; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   iPTMnet; Q86M34; -.
DR   VEuPathDB; AmoebaDB:EHI5A_038640; -.
DR   VEuPathDB; AmoebaDB:EHI7A_122380; -.
DR   VEuPathDB; AmoebaDB:EHI8A_195650; -.
DR   VEuPathDB; AmoebaDB:EHI_007330; -.
DR   VEuPathDB; AmoebaDB:KM1_199570; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   OMA; QYWVDHA; -.
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; 3.30.379.10; -; 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; IPR029019; HEX_eukaryotic_N.
DR   PANTHER; PTHR22600; PTHR22600; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF14845; Glycohydro_20b2; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000269|PubMed:15555733"
FT   CHAIN           14..565
FT                   /note="Beta-hexosaminidase subunit beta"
FT                   /id="PRO_0000012012"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:15555733"
SQ   SEQUENCE   565 AA;  64372 MW;  DABBBA0B932BBA4F CRC64;
     MIVLLLLISY CFAGNGVNVK NQLLLMPYPT TVNAQFGSND CVEATSNIKM VLSNNCQNDP
     NCLSFMTFNF NHTITYPLQR QRNLEDFRVS IFAPIDIEEM KGNVVYSANT VNIELTGNNI
     EEIYPPLKIG IDESYSLDVT KEGIKISATT VYGARLGLET LIQMLRPYQG KYIIKHIPIM
     IEDKPRLQWR GLMIDVARNS FSRSAFVKII NAMAAIKANV LHIHLSDAQT FMFESKEYPE
     LSKKGAFFQN KVLTQSFIKQ LVQYGAKRGV IVYPEIDTPA HTASWNAGYP GVVADIWDYI
     VSSSMRYGEN VLALNPANEK TFSIIDALMK EMGEVFGNDY VHFGGDEVWT GAWSKAKEYP
     AILEWMNKKG INTLKELEAY FNKYAQEQII KNGKTPVCWE EVYQKGSADK KTIIQVWNNV
     NLLKEAATAG YKVILSAGYY LDMQMPLCSD YVADSCTNPN HMWVWTNRDM YRNDPIKELD
     YATKQNVLGG EACSWDESVD EQNFFDRVFQ RFSAVAERFW SSEDITDPES HEVRANYVRC
     LGLRRNFLKG TGPLYHSYCQ LPEDI