ID A0A0N5A0H1_PARTI Unreviewed; 550 AA.
AC A0A0N5A0H1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001491800.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001491800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 ECO:0000256|PIRNR:PIRNR001093};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR AlphaFoldDB; A0A0N5A0H1; -.
DR STRING; 131310.A0A0N5A0H1; -.
DR WBParaSite; PTRK_0001491800.1; PTRK_0001491800.1; PTRK_0001491800.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..150
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 174..510
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 331
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 550 AA; 64262 MW; 04FDFAB3A5A9757B CRC64;
MKYTQSYIIF LLINFYLIYV LTYKQNGKWL PIPTDGEIWP KPYFYNYFEE RLIVSPGMIK
LSFENNKNCK LFESLFNRYS EKYFFPFKIK SNGTYSISLE VKILSCPKYN EYPQIGMDES
YELVINSNRT AKIVANEAWG AIKGLESFSQ VITFDDKKNI YKIRTLNVID KPRFKVRGFL
IDTSRHFLPV YVIKRHLDLM SMNKMNLLHW HIVDTQSFPY QSKIYPELSN QGAFTLKHIY
TRGNIQSIIE YAKTLGIVVM PEFDTPGHMG SWNGIDGLLS QCYDKDGRKS ITIQPNLIDL
SEKKNFDVLK SLFKEIKTLF KSSYIHLGGD EVEFWEESCW FRNPKIIQFM KNMGFGNEKK
LLEEWYITQL SQIVSSVNKN WSQIYWQEVF DNSKVPDNAI VHLWKGRTKE EIYKALNNIT
EKGYNVIISS GWYLNYIHYG SDWKQASKIG DSVSPALYDI DIQGFNGTES QKARVIGGIA
AMWGEYIDQT NIESTSWPRG SAVAEKLWSP QNETIKADDQ IQRFREQRCR MIHRGYQIAP
TDGPDFCLLN
//
