ID B3RUQ5_TRIAD Unreviewed; 373 AA.
AC B3RUQ5;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE Flags: Fragment;
GN ORFNames=TRIADDRAFT_2382 {ECO:0000313|EMBL:EDV25367.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV25367.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV25367.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25367.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; DS985244; EDV25367.1; -; Genomic_DNA.
DR RefSeq; XP_002111400.1; XM_002111364.1.
DR AlphaFoldDB; B3RUQ5; -.
DR STRING; 10228.B3RUQ5; -.
DR EnsemblMetazoa; TriadT2382; TriadP2382; TriadG2382.
DR GeneID; 6752613; -.
DR KEGG; tad:TRIADDRAFT_2382; -.
DR CTD; 6752613; -.
DR eggNOG; ENOG502QRCP; Eukaryota.
DR HOGENOM; CLU_019666_0_0_1; -.
DR InParanoid; B3RUQ5; -.
DR OMA; VWNYLDT; -.
DR OrthoDB; 2876932at2759; -.
DR PhylomeDB; B3RUQ5; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015929; F:hexosaminidase 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 CDD; cd06565; GH20_GcnA-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR038901; HEXDC-like.
DR PANTHER; PTHR21040:SF8; BCDNA.GH04120; 1.
DR PANTHER; PTHR21040; UNCHARACTERIZED; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 58..223
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV25367.1"
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:EDV25367.1"
SQ SEQUENCE 373 AA; 42455 MW; F9BE126B8256E314 CRC64;
ERKFPGHRVI HLDLKGAPPK MTYYKKLFPF LRSLGATGVL IEYEDMFPYK DNLKVLARTD
AYTESEVNAI VQLAEEFKLL VIPLIQTFGH LEFMLKHQQF KHLRALSTSK KALCPCQNSS
LPILLDMAKQ VIALHPNTKY LHIGGDEIYD LMKCTKCKAL AYKKHDMYLL HMVPLLTEIK
SSWPELTVLM WDDMLRSWSV DQMLTLQNLA TPMVWAYEEN LSKYFPQTMW KNYKQVFGSV
WIASAFKGAL RKDTDIVPLN KHIENQLQWL KIISNLDGME IPGIAITGWS RFDHFSPLCE
LLPAGLPSLA LCLTALDRGS VNPEVIHTVS VDALGCAGKI YDDSSGTYQV QKCGFPGSDV
FLIVSRLDLL RNE
//
