HEXA2_DICDI
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 25-MAY-2022, entry version 107.
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 (Slime mold).
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 RefSeq; XP_640110.1; XM_635018.1.
DR AlphaFoldDB; Q54SC9; -.
DR SMR; Q54SC9; -.
DR STRING; 44689.DDB0304517; -.
DR PaxDb; Q54SC9; -.
DR EnsemblProtists; EAL66129; EAL66129; DDB_G0282539.
DR GeneID; 8623642; -.
DR KEGG; ddi:DDB_G0282539; -.
DR dictyBase; DDB_G0282539; nagB.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_3_1; -.
DR InParanoid; Q54SC9; -.
DR OMA; QNIFCAG; -.
DR PhylomeDB; Q54SC9; -.
DR Reactome; R-DDI-1660662; Glycosphingolipid metabolism.
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 PRO; PR:Q54SC9; -.
DR Proteomes; UP000002195; Chromosome 3.
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 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..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
