ID   HEXA_CAEBR              Reviewed;         552 AA.
AC   Q619W7; A8XJ97;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Beta-hexosaminidase A;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   Flags: Precursor;
GN   Name=hex-1 {ECO:0000250|UniProtKB:Q22492}; ORFNames=CBG14058;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and a
CC       variety of other molecules containing terminal N-acetyl hexosamines.
CC       Degrades chitotriose (By similarity). {ECO:0000250|UniProtKB:Q22492}.
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:0000250|UniProtKB:P06865};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P06865}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000255}.
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DR   EMBL; HE600983; CAP32722.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q619W7; -.
DR   SMR; Q619W7; -.
DR   STRING; 6238.CBG14058; -.
DR   EnsemblMetazoa; CBG14058.1; CBG14058.1; WBGene00034691.
DR   WormBase; CBG14058; CBP29009; WBGene00034691; Cbr-hex-1.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   InParanoid; Q619W7; -.
DR   OMA; GHDVVMC; -.
DR   OrthoDB; 545162at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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; ISS:UniProtKB.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR   GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.379.10; -; 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; PTHR22600; 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; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..552
FT                   /note="Beta-hexosaminidase A"
FT                   /id="PRO_0000312664"
FT   ACT_SITE        322
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   552 AA;  63880 MW;  F51F5E37E49720A0 CRC64;
     MRLIVLSLLF TSTLAWFYGR DEPDRWSVGG VWPLPQKIIY GSKNRTLTYD KIGIDLGDKK
     DCDVLLAMAD NYMNKWLFPY PVEMKTGGTE DFIITVTVKE ECPGGPPVHG ASEEYLLRVS
     VSEAVINAQT VWGALRAMET LSHLVFYDQK SQEYQIRTAE IFDKPRFPVR GIMIDSSRHF
     LSLNVIKRQL EIMSMNKLNV LHWHLVDSES FPYTSQKFPE LHGVGAYSPR HVYSREDISE
     VIAFARLRGI RVIPEFDLPG HTSSWKGRKG FLTECFDEKG EETFLPNLVD PMNDANFDFL
     AEFLEEVTET FPDQFLHLGG DEVSDYIVEC WVRNKKIRKF MDEKGFGNNT VLLENYFFEK
     LFSIVEKLKL KRKPIFWQEV FDNNIPDPNS IIHIWKGNTH EEIYEQVKNI TSKNFPVIVS
     ACWYLNYIKY GADWRDEIRG TAPSNSRYYY CDPTSFNGTD TQKNLVLGGI AAIWGELVDN
     TNIEARLWPR ASAAAERLWS PAEKTQKAEN AWPRMHELRC RLVSRGYRIQ PNNNPDYCPF
     EFDEPPATKS EL