ID   HEXA2_DICDI             Reviewed;         541 AA.
AC   Q54SC9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   RecName: Full=Beta-hexosaminidase subunit A2;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit A2;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit A2;
DE   Flags: Precursor;
GN   Name=hexa2; ORFNames=DDB_G0282539;
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; AAFI02000047; EAL66129.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54SC9; -.
DR   SMR; Q54SC9; -.
DR   FunCoup; Q54SC9; 106.
DR   STRING; 44689.Q54SC9; -.
DR   GlyCosmos; Q54SC9; 5 sites, No reported glycans.
DR   GlyGen; Q54SC9; 5 sites.
DR   PaxDb; 44689-Q54SC9; -.
DR   KEGG; ddi:DDB_G0282539; -.
DR   dictyBase; DDB_G0282539; nagB.
DR   VEuPathDB; AmoebaDB:DDB_G0282539; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_3_1; -.
DR   InParanoid; Q54SC9; -.
DR   OMA; KMWPRAA; -.
DR   PhylomeDB; Q54SC9; -.
DR   Reactome; R-DDI-2022857; Keratan sulfate degradation.
DR   Reactome; R-DDI-2024101; CS/DS degradation.
DR   Reactome; R-DDI-2160916; Hyaluronan degradation.
DR   Reactome; R-DDI-9840310; Glycosphingolipid catabolism.
DR   PRO; PR:Q54SC9; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase 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   FunFam; 3.20.20.80:FF:000063; Beta-hexosaminidase; 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; GH20.
DR   InterPro; IPR015883; GH20_cat.
DR   InterPro; IPR017853; GH_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   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..541
FT                   /note="Beta-hexosaminidase subunit A2"
FT                   /id="PRO_0000331236"
FT   ACT_SITE        314
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   541 AA;  61533 MW;  F670234F1DD3D075 CRC64;
     MINKFLTIFL IFSIVIIKVL SQSSNEQPLN VVPYPQEVTM IGCNIPLSVG SISIKSNIES
     TILSISISRY QSLFFPFVSN NVLKDSSSNI ELSLIIASDD ETLELGIDES YFLLVNQDTY
     QIKANTIYGA MRGLETFKQM VVYDVVENSY SLTCAEVVDY PTYQWRGLLV DNARHFLPKN
     MVLHIIDSMG YNKFNTMHWH LIDTVAFPVE SKTYPKLTEA LLGPGAIITH DDILEVVAYA
     KTYGIRVIPE FDVPGHSASW GVGYPELLSN CPGYPQSSIP LDCSNPYTYS FLENFFSEIA
     PLFQDSYFHT GGDELVIDCW ANDTSIQKWM KTNNYNTSDA FQYFEDQLDV ILKSINRTKI
     AWNDVLQHGV KFDKETTLVQ TWTNINDLRD VLAAGYKTIT SFFFYLDRQS PTGNHYHYEW
     QDTWEDFYAS DPRLNITSNA ENILGGEATM FGEQVSTVNW DARVWPRAIG ISERLWSATE
     INNITLALPR IGQFSCDMSR RGISSGPLFP DFCSLPDDLS FSFKPVYQLS KDEIKLILKK
     K
//