ID   HEXA_ENTH1              Reviewed;         538 AA.
AC   P49009; C4LSY3; Q70FJ0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2023, sequence version 3.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Beta-hexosaminidase subunit alpha;
DE            EC=3.2.1.52 {ECO:0000269|PubMed:15555733};
DE   AltName: Full=Beta-GlcNAcase subunit alpha;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit alpha {ECO:0000303|PubMed:15555733};
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit alpha;
GN   Name=HEXA {ECO:0000303|PubMed:15555733}; Synonyms=BEX-1, HEX-A1;
GN   ORFNames=EHI_148130 {ECO:0000312|EMBL:EAL52144.2};
OS   Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381 {ECO:0000312|EMBL:EAL52144.2};
RN   [1] {ECO:0000312|EMBL:CAE46968.1, ECO:0000312|EMBL:CAG23943.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   INTERACTION WITH HEXB, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:CAE46968.1,
RC   ECO:0000312|EMBL:CAG23943.1};
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] {ECO:0000312|EMBL:EAL52144.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:EAL52144.2};
RX   PubMed=15729342; DOI=10.1038/nature03291;
RA   Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA   Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA   Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA   Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA   Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA   Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA   Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA   Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA   Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA   Barrell B.G., Fraser C.M., Hall N.;
RT   "The genome of the protist parasite Entamoeba histolytica.";
RL   Nature 433:865-868(2005).
RN   [3] {ECO:0000312|EMBL:AAA80165.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-538.
RC   STRAIN=ATCC 30459 / HM-1:IMSS / ABRM {ECO:0000312|EMBL:AAA80165.1};
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: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or
CC       sulfated N-acetyl-D-hexosamine of glycoconjugates (PubMed:15555733).
CC       May contribute to amoebic pathogenicity and may be involved in the
CC       destruction of extracellular matrix components (Probable).
CC       {ECO:0000269|PubMed:15555733, ECO:0000305|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         Evidence={ECO:0000269|PubMed:15555733};
CC   -!- SUBUNIT: Heterodimer of one alpha subunit and one beta subunit.
CC       {ECO:0000269|PubMed:15555733}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC       {ECO:0000269|PubMed:15555733}. Secreted {ECO:0000269|PubMed:15555733}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in trophozoites (at protein level).
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; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAE46968.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAG23943.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ582954; CAE46968.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ634053; CAG23943.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DS571146; EAL52144.2; -; Genomic_DNA.
DR   EMBL; U09735; AAA80165.1; ALT_INIT; mRNA.
DR   RefSeq; XP_657529.2; XM_652437.2.
DR   AlphaFoldDB; P49009; -.
DR   SMR; P49009; -.
DR   STRING; 5759.C4LSY3; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   GlyCosmos; P49009; 1 site, No reported glycans.
DR   iPTMnet; P49009; -.
DR   EnsemblProtists; rna_EHI_148130-1; rna_EHI_148130-1; EHI_148130.
DR   GeneID; 3411822; -.
DR   KEGG; ehi:EHI_148130; -.
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   HOGENOM; CLU_007082_0_3_1; -.
DR   OMA; NYCVEPP; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000001926; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   CDD; cd06562; GH20_HexA_HexB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..538
FT                   /note="Beta-hexosaminidase subunit alpha"
FT                   /id="PRO_0000012011"
FT   ACT_SITE        317
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06865"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   538 AA;  61054 MW;  3DE83EA6B04E21C8 CRC64;
     MPYPSSVSFQ WKSPLAIALT SSIQLNVKST CNTDCMNFLK SNFNHTISFP LQQQTGLQDF
     KVSLFKEIDL PRITPSVSSV ITDVVVELSS SNPMPKLQIG FDESYILEVT TNSISIKAVT
     VYGARHAFET LLQLIRISSN KFVISQLPIK ISDAPRFKWR GLMVDPSRNP LSPLMFKRII
     DTLASVKANV LHIHLSDAQT FVFESKKYPL LHQKGMYDES FVLTQSFLRE LAQYGANRGV
     IVYGEIDTPA HTASWNLGYP GVVANCWDYI VSTSMRYGEN VLSLNPANPN TFPIIDALMK
     ELSDTFGTDY VHVGGDEVWT SGWSKSKEYS DIQKFMKSKG LNSLTELEGY FNKYAQEQVI
     HNGKHPVVWE EVFKKGNADK NTIIQVWDDI RLLQQVVNSG YKAIFSAGFY LDKQMPLCNS
     YDSSTCVNTH SMWVWTNRDM YDNDPVKSLS SSEKENVLGG EGCSWGESTD EQNFFDRVFQ
     RYSAIAERLW SKESVVDKES HEVRANYLRC LDVRRDIMKG TGPLYHSFCQ LPKKEKSN
//