HEXB2_DICDI
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 25-MAY-2022, entry version 106.
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 (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; AAFI02000103; EAL63638.1; -; Genomic_DNA.
DR RefSeq; XP_637108.1; XM_632016.1.
DR AlphaFoldDB; Q54K56; -.
DR SMR; Q54K56; -.
DR STRING; 44689.DDB0304516; -.
DR PaxDb; Q54K56; -.
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; QNENECP; -.
DR PhylomeDB; Q54K56; -.
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: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 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..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
