HEXB1_DICDI
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 25-MAY-2022, entry version 97.
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 (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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000103; EAL63607.1; -; Genomic_DNA.
DR RefSeq; XP_637109.1; XM_632017.1.
DR AlphaFoldDB; Q54K55; -.
DR SMR; Q54K55; -.
DR STRING; 44689.DDB0304520; -.
DR PaxDb; Q54K55; -.
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; GHDVVMC; -.
DR PhylomeDB; Q54K55; -.
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: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 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..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
