ID   HEXB2_DICDI             Reviewed;         564 AA.
AC   Q54K56;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Beta-hexosaminidase subunit B2;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit B2;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit B2;
DE   Flags: Precursor;
GN   Name=hexb2; ORFNames=DDB_G0287659;
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; EAL63638.1; -; Genomic_DNA.
DR   RefSeq; XP_637108.1; XM_632016.1.
DR   AlphaFoldDB; Q54K56; -.
DR   SMR; Q54K56; -.
DR   STRING; 44689.Q54K56; -.
DR   GlyCosmos; Q54K56; 9 sites, No reported glycans.
DR   PaxDb; 44689-DDB0304516; -.
DR   EnsemblProtists; EAL63638; EAL63638; DDB_G0287659.
DR   GeneID; 8626203; -.
DR   KEGG; ddi:DDB_G0287659; -.
DR   dictyBase; DDB_G0287659; nagD.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   InParanoid; Q54K56; -.
DR   OMA; GHDVVMC; -.
DR   PhylomeDB; Q54K56; -.
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:Q54K56; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..564
FT                   /note="Beta-hexosaminidase subunit B2"
FT                   /id="PRO_0000331238"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   564 AA;  64566 MW;  0C65D857428ABC9E CRC64;
     MKLKFIFLIL FFIIGNSIGI KISKEINKIK LNDISIDGEI LLNKSSDSSS SQSSKIINIW
     PMPKKVLNGD ITVYISPHFQ FTTNLTKSTT LKKAMDRYYK LIFTEDSKSH SGISILNEIK
     ILVKSEDETL QIGFDESYEI YIDDSGDDGG KIIAETVYGA IRGLETLYQM IGFDYQREYY
     QIKHCPWIIQ DSPRYPHRGV MLDTSRHFYS VDVLKEFIEA LAYNKFNVFH WHAVDSQSFP
     LTSTTFPKIT KGSWSSQEIY STRDIKEIIQ HAKEYGIRVE LEIDMPGHAY SWGIGYPSVL
     PANFSHSIQC QQPCPTECNI PLDVSSKESY VIAMGLLEEF NGASMFNESF FHIGGDEVAY
     SCWNNSLRIV DWMKRENISS FQDAAIFFEI KAIEQLIQLG KTPVMWEDAY LLFGSSGITE
     KLPEEVVVQI YHDPLLALNT TRDGYKTLQS PYWPYYLDNP SVDWEKVYEF EPSNGIHEKR
     LRLLLGGETC MWSELVDASN LFAKVFPRAF ATAERLWFSI ENSNSTTFAK PRLERFRCFL
     LERGIGAAPL NSTSPDDPNS CYSS
//