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Database: UniProt
Entry: A0A0V1HNH2_9BILA
LinkDB: A0A0V1HNH2_9BILA
Original site: A0A0V1HNH2_9BILA 
ID   A0A0V1HNH2_9BILA        Unreviewed;       567 AA.
AC   A0A0V1HNH2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   Flags: Fragment;
GN   Name=Hexb {ECO:0000313|EMBL:KRZ12001.1};
GN   ORFNames=T11_2118 {ECO:0000313|EMBL:KRZ12001.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12001.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ12001.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12001.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001231};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ12001.1}.
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DR   EMBL; JYDP01000044; KRZ12001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HNH2; -.
DR   STRING; 268475.A0A0V1HNH2; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001093-2};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          66..180
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          205..526
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
FT   DISULFID        95..137
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        314..366
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        543..561
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ12001.1"
SQ   SEQUENCE   567 AA;  65199 MW;  60C01D484AF2AD09 CRC64;
     LHMPLRQVIA AYETIRYCSF PPGVIKQSKT GIIMRLSTLY FIVLLNTGFV KLSISKFISS
     RTYGIPWPMP HEFTLDNGNF SLLQESFKFY TTYSCDILAN AMQFYLKILF PPSDSSTDET
     SELLPFTTLK IVVHMPCPPG YPTSNMIENY TLSLWPNGTG LLESLQVWGA LRGLETFSQL
     VIPADPVEHT TTMLRSANIN DSPRFPHRGI LLDTSRHFIP VDVIKTQLEL MAQNKFNVFH
     WHIVDDPSFP YQSDSFPNLS NKGAFSNQRI YKKLDILKVI NYARLWGIRV IAEFDTPCHV
     QSWADAMENL TSSCDISHLY FDPLTGSLDP TRPETYSFMK TLLQEVLNDF PDEHFHLGGD
     ECDLGCWDYN SAIRTFKKEM NFTTLKEVQS YYLNKLLDLV MEIRPNLIPI LWEDGLSDSI
     KYSDKLIIQM WLGNTRNQQR SRLANITARG YRALVSSCWY LNIIKYGIDW PEYYDCDPRD
     FNGTLEQKSL VLGGEACMWG EHVDSSNLTP RLWPRAAAVG ERLWSMEMKR NESTAQRLEN
     HRCRLLARGY TVEPVNGPGY CYEVAKL
//
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