ID   HEXB1_DICDI             Reviewed;         560 AA.
AC   Q54K55;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Beta-hexosaminidase subunit B1;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit B1;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit B1;
DE   Flags: Precursor;
GN   Name=hexb1; ORFNames=DDB_G0287597;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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).
CC   -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and a
CC       variety of other molecules containing terminal N-acetyl hexosamines.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; AAFI02000103; EAL63607.1; -; Genomic_DNA.
DR   RefSeq; XP_637109.1; XM_632017.1.
DR   AlphaFoldDB; Q54K55; -.
DR   SMR; Q54K55; -.
DR   STRING; 44689.Q54K55; -.
DR   GlyCosmos; Q54K55; 11 sites, No reported glycans.
DR   PaxDb; 44689-DDB0304520; -.
DR   EnsemblProtists; EAL63607; EAL63607; DDB_G0287597.
DR   GeneID; 8626204; -.
DR   KEGG; ddi:DDB_G0287597; -.
DR   dictyBase; DDB_G0287597; nagC.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   InParanoid; Q54K55; -.
DR   OMA; STSYYNW; -.
DR   PhylomeDB; Q54K55; -.
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-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-9840310; Glycosphingolipid catabolism.
DR   PRO; PR:Q54K55; -.
DR   Proteomes; UP000002195; Chromosome 5.
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: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   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..560
FT                   /note="Beta-hexosaminidase subunit B1"
FT                   /id="PRO_0000331237"
FT   ACT_SITE        359
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   560 AA;  64555 MW;  DF3700F79651C682 CRC64;
     MIILKRNIVF LLIIIIVLGI FIATSIEIKN YKLSLNQNKN EISKNPPIWP APFYGQFGNN
     SILISKEFNF TIISDSTLLL NKTLSKYYNL IFTQDNLINS SSNTLNKLNI NLKSKNEILK
     FGFDESYKLI IKNNENSKLE GNTVYGIMRG LETFYQLIKY NFSDNSYFIE NCLPLIINDK
     PRFPHRGVML DTSRHFYSVD TILKVIESLS YNKFNTLHWH IIDSQSFPLS SKSYPNLING
     AWSKSEIYSY HDIKRIIKYG KENGIRIQLE IDMPGHAKSW SVGYPDLLPH GWNDSTTTIK
     CPDYDVPLDP SSPLSLPISF GLLSEFSGTD YGYNPNYDDK SNNLFNLTVD DLFHVGGDEI
     EYQCWNNSKR IKDWMNENNL KTFQDVAKQF QLKIIKQLLK IGKIPVLWED TFQLFYKDLP
     KDVIVEIYHD QSTAINATNN GYKIISSIAR YWYLEYSYSN WIRAYNFEPT LNISKSNIHL
     VLGGEGAIWS ESIDSSNLFQ KLYPTSSAIA ERLWSPIYYT NLLNAKSRLQ SFRCSLLKRG
     INSAPLNNSS PLSAFSCYNS
//