ID   HEXA1_DICDI             Reviewed;         532 AA.
AC   P13723; Q54KX2;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Beta-hexosaminidase subunit A1;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit A1;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit A1;
DE   Flags: Precursor;
GN   Name=hexa1; Synonyms=nagA; ORFNames=DDB_G0287033;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 105-113; 260-276 AND
RP   295-306, FUNCTION, PTM, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=2972716; DOI=10.1016/s0021-9258(18)37465-9;
RA   Graham T.R., Zassenhaus H.P., Kaplan A.;
RT   "Molecular cloning of the cDNA which encodes beta-N-acetylhexosaminidase A
RT   from Dictyostelium discoideum. Complete amino acid sequence and homology
RT   with the human enzyme.";
RL   J. Biol. Chem. 263:16823-16829(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=NC-4;
RX   PubMed=640375; DOI=10.1093/genetics/88.2.277;
RA   Loomis W.F.;
RT   "Genetic analysis of the gene for N-acetylglucosaminidase in Dictyostelium
RT   discoideum.";
RL   Genetics 88:277-284(1978).
CC   -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and a
CC       variety of other molecules containing terminal N-acetyl hexosamines.
CC       This enzyme plays a role during the slug stage of development in the
CC       maintenance of pseudoplasmodia of normal size.
CC       {ECO:0000269|PubMed:2972716}.
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   -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:640375}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2972716}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2972716}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; J04065; AAA33230.1; -; mRNA.
DR   EMBL; AAFI02000096; EAL63881.1; -; Genomic_DNA.
DR   PIR; A30766; A30766.
DR   RefSeq; XP_637398.1; XM_632306.1.
DR   AlphaFoldDB; P13723; -.
DR   SMR; P13723; -.
DR   STRING; 44689.P13723; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   GlyCosmos; P13723; 4 sites, No reported glycans.
DR   PaxDb; 44689-DDB0191256; -.
DR   EnsemblProtists; EAL63881; EAL63881; DDB_G0287033.
DR   GeneID; 8625929; -.
DR   KEGG; ddi:DDB_G0287033; -.
DR   dictyBase; DDB_G0287033; nagA.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   InParanoid; P13723; -.
DR   OMA; KMWPRAA; -.
DR   PhylomeDB; P13723; -.
DR   Reactome; R-DDI-2022857; Keratan sulfate degradation.
DR   Reactome; R-DDI-2024101; CS/DS degradation.
DR   Reactome; R-DDI-2160916; Hyaluronan uptake and degradation.
DR   Reactome; R-DDI-9840310; Glycosphingolipid catabolism.
DR   PRO; PR:P13723; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:dictyBase.
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: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:SF54; BETA-HEXOSAMINIDASE SUBUNIT A1-RELATED; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..532
FT                   /note="Beta-hexosaminidase subunit A1"
FT                   /id="PRO_0000012010"
FT   ACT_SITE        308
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   532 AA;  59788 MW;  CE651DD79F456514 CRC64;
     MIKKIILFFA VLIAIVIGQQ PLNVVPYPQQ VSIGTCVIPV APGSILIESN IESATFSVSM
     DRYTNLFFPF SNESEPSSNE SFLLSVTIYS DDETLQLGID ESYSLSIEQG SYQLKATNIY
     GAMRGLETFK QLIVYNELEN SYSIVCVSIS DSPRYPWRGF MVDSARHYIP KNMILHMIDS
     LGFSKFNTLH WHMVDAVAFP VESTTYPDLT KGAFSPSATF SHDDIQEVVA YAKTYGIRVI
     PEFDIPGHAA AWGIGYPELV ATCPDYAANV NNIPLDISNP ATFTFIQNLF TEIAPLFIDN
     YFHTGGDELV TGCWLEDPAI ANWMTKMGFS TTDAFQYFEN NLDVTMKSIN RTKITWNDPI
     DYGVQLNPET LVQVWSSGSD LQGIVNSGYK ALVSFAWYLD KQNPDNNIHY EWQDTWQDFY
     AADPTNNIST NAENIIGGEA TMWAEQINQV NWDVRVWPRA IGIAERLWSA QSVNSVSLAL
     PRIGHFTCDL SRRGIQSGPL FPDYCPMQDD LVFTMKPNTK LSKSEIKLIL NK
//