ID A0A093EMN6_TYTAL Unreviewed; 380 AA.
AC A0A093EMN6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Beta-hexosaminidase subunit beta {ECO:0000256|ARBA:ARBA00040637};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE AltName: Full=Beta-N-acetylhexosaminidase subunit beta {ECO:0000256|ARBA:ARBA00042342};
DE AltName: Full=N-acetyl-beta-glucosaminidase subunit beta {ECO:0000256|ARBA:ARBA00042832};
DE Flags: Fragment;
GN ORFNames=N341_04242 {ECO:0000313|EMBL:KFV44429.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV44429.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV44429.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV44429.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-
CC iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-
CC (1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-
CC sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064;
CC Evidence={ECO:0000256|ARBA:ARBA00023541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385;
CC Evidence={ECO:0000256|ARBA:ARBA00023541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-
CC sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D-
CC 3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-
CC acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164;
CC Evidence={ECO:0000256|ARBA:ARBA00023953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277;
CC Evidence={ECO:0000256|ARBA:ARBA00023953};
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 Evidence={ECO:0000256|ARBA:ARBA00001231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-
CC sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-
CC L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-
CC GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565,
CC ChEBI:CHEBI:152566; Evidence={ECO:0000256|ARBA:ARBA00023505};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373;
CC Evidence={ECO:0000256|ARBA:ARBA00023505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3
CC (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065,
CC ChEBI:CHEBI:71502; Evidence={ECO:0000256|ARBA:ARBA00023546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941;
CC Evidence={ECO:0000256|ARBA:ARBA00023546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-
CC galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218;
CC Evidence={ECO:0000256|ARBA:ARBA00023512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969;
CC Evidence={ECO:0000256|ARBA:ARBA00023512};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC granule {ECO:0000256|ARBA:ARBA00037865}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; KK372729; KFV44429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093EMN6; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF38; BETA-HEXOSAMINIDASE SUBUNIT BETA; 1.
DR Pfam; PF00728; Glyco_hydro_20; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190}.
FT DOMAIN 51..367
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV44429.1"
FT NON_TER 380
FT /evidence="ECO:0000313|EMBL:KFV44429.1"
SQ SEQUENCE 380 AA; 43681 MW; 398CA8E38D4DF75C CRC64;
HLTVTEPVAI LKADEVWGAL RGLETFSQLV HEDDYGSFLV NESEIDDFPR FAHRGILLDT
SRHYLPLKSI LTNLDAMAFN KFNVLHWHIV DDQSFPYQSI YFPELSDKGA YSYNHIYTPT
DIRLVIEYAR LRGIRVIPEF DTPGHTQSWG KGQKDLLTPC YSGEQPTGSF GPVNPILNTT
YDFMTKFFKE ISSVFPDAYI HLGGDEVNFD CWKSNPEVKE FMKKQGFGTD YAKLESYYIQ
KILDIVFSYN KGYVVWQEVF DNKAQLKPDT VVQVWMENNY AHELSSVTGA GFTAILAAPW
YLDYISYGQD WKKYYSVEPL NFPGSEKQKK LLIGGEACLW GEFVDATNLT PRLWPRASAV
GERLWSSRDV TNLHDAYNRL
//