ID B3S8X9_TRIAD Unreviewed; 482 AA.
AC B3S8X9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=TRIADDRAFT_60782 {ECO:0000313|EMBL:EDV20849.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV20849.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV20849.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV20849.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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 EMBL; DS985257; EDV20849.1; -; Genomic_DNA.
DR RefSeq; XP_002116790.1; XM_002116754.1.
DR AlphaFoldDB; B3S8X9; -.
DR STRING; 10228.B3S8X9; -.
DR EnsemblMetazoa; TriadT60782; TriadP60782; TriadG60782.
DR GeneID; 6758002; -.
DR KEGG; tad:TRIADDRAFT_60782; -.
DR CTD; 6758002; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_0_1; -.
DR InParanoid; B3S8X9; -.
DR OMA; HYLPVTN; -.
DR OrthoDB; 178991at2759; -.
DR PhylomeDB; B3S8X9; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IBA:GO_Central.
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 GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..482
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002798513"
FT DOMAIN 32..91
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 112..429
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 482 AA; 55755 MW; F5E4EDCCA0937D66 CRC64;
MASIQIIILI TLLCQRWCDA GAAVNPNQDA IKAVGNLTKL FVQIDDVSAN LTLNSDESYS
LSIHAHPQPV AFLHAKQTWG ALRGLESFSQ LIDATYDGFF IQETKIVDYP RFKYRGVMLD
SARHYLTLDV ILQNLDAMSY NKFNVFHWHI VDDQSFPFVS LTYPQLSQHG SYTPRHVYTP
DDVQMVIEYA RDRGIRVIVE FDTPGHSSSW RSIPNFLTPC YSKNGVPNGQ FGPINPILNS
TYTILEDFFR EIKKRFPDQY VHLGGDEVNF SCWQSNPDIQ NFMTQHGFGD HYELLEQYYE
HNLVTIMEKI GLRYIIWQDV VDNNVKVDPN TVVQVWKTSP SYKAELAKVT KMNLQTILSS
CWYLNYIGYG RDWERFYRCD PQDFKGTQQQ KNLVIGGEAC IWGEYVDSTN LMERFWPRAS
AVSERLWSSA KVTNVDAALP RIDHHRCYQL IRRGLRAQPI NGYSFCQAEY NVVMNHLDRD
EL
//
