ID   HEXA_ENTHI              Reviewed;         564 AA.
AC   P49009; Q70FJ0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Beta-hexosaminidase subunit alpha;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-GlcNAcase subunit alpha;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit alpha;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit alpha;
DE   Flags: Precursor;
GN   Name=HEXA; Synonyms=BEX-1, HEX-A1;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP   AND INTERACTION WITH HEXB.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RA   Scholze H.H.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-564.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=7581340; DOI=10.1111/j.1550-7408.1995.tb05919.x;
RA   Beanan M.J., Bailey G.B.;
RT   "The primary structure of an Entamoeba histolytica beta-hexosaminidase A
RT   subunit.";
RL   J. Eukaryot. Microbiol. 42:632-636(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA80165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ582954; CAE46968.1; -; Genomic_DNA.
DR   EMBL; AJ634053; CAG23943.1; -; Genomic_DNA.
DR   EMBL; U09735; AAA80165.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; P49009; -.
DR   SMR; P49009; -.
DR   STRING; 5759.rna_EHI_148130-1; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   iPTMnet; P49009; -.
DR   VEuPathDB; AmoebaDB:EHI5A_038640; -.
DR   VEuPathDB; AmoebaDB:EHI7A_122380; -.
DR   VEuPathDB; AmoebaDB:EHI8A_195650; -.
DR   VEuPathDB; AmoebaDB:EHI_148130; -.
DR   VEuPathDB; AmoebaDB:KM1_199570; -.
DR   eggNOG; KOG2499; Eukaryota.
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   Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000250"
FT   CHAIN           15..564
FT                   /note="Beta-hexosaminidase subunit alpha"
FT                   /id="PRO_0000012011"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:15555733"
SQ   SEQUENCE   564 AA;  63935 MW;  8EFE1D34609C86A4 CRC64;
     MLFIFIVFIS SVFAGNGLNV QNQLLLMPYP SSVSFQWKSP LAIALTSSIQ LNVKSTCNTD
     CMNFLKSNFN HTISFPLQQQ TGLQDFKVSL FKEIDLPRIT PSVSSVITDV VVELSSSNPM
     PKLQIGFDES YILEVTTNSI SIKAVTVYGA RHAFETLLQL IRISSNKFVI SQLPIKISDA
     PRFKWRGLMV DPSRNPLSPL MFKRIIDTLA SVKANVLHIH LSDAQTFVFE SKKYPLLHQK
     GMYDESFVLT QSFLRELAQY GANRGVIVYG EIDTPAHTAS WNLGYPGVVA NCWDYIVSTS
     MRYGENVLSL NPANPNTFPI IDALMKELSD TFGTDYVHVG GDEVWTSGWS KSKEYSDIQK
     FMKSKGLNSL TELEGYFNKY AQEQVIHNGK HPVVWEEVFK KGNADKNTII QVWDDIRLLQ
     QVVNSGYKAI FSAGFYLDKQ MPLCNSYDSS TCVNTHSMWV WTNRDMYDND PVKSLSSSEK
     ENVLGGEGCS WGESTDEQNF FDRVFQRYSA IAERLWSKES VVDKESHEVR ANYLRCLDVR
     RDIMKGTGPL YHSFCQLPKK EKSN