ID A0A2I0U9D6_LIMLA Unreviewed; 558 AA. AC A0A2I0U9D6; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 29-SEP-2021, entry version 14. DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093}; DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093}; GN ORFNames=llap_7024 {ECO:0000313|EMBL:PKU42669.1}; OS Limosa lapponica baueri. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Charadriiformes; Scolopacidae; Limosa. OX NCBI_TaxID=1758121 {ECO:0000313|EMBL:PKU42669.1}; RN [1] {ECO:0000313|EMBL:PKU42669.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BTGAFAM01 {ECO:0000313|EMBL:PKU42669.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PKU42669.1}; RA Han C.G.; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PKU42669.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BTGAFAM01 {ECO:0000313|EMBL:PKU42669.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PKU42669.1}; RA Lima N.C.B., Parody-Merino A.M., Battley P.F., Fidler A.E., Prosdocimi F.; RT "Genome sequence of the Bar-tailed Godwit (Limosa lapponica baueri)."; RL Submitted (JAN-2018) 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 ECO:0000256|PIRNR:PIRNR001093}; 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=ganglioside GM2 (d18:1(4E)) + H2O = 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=ganglioside GM2 + H2O = 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: Lysosome {ECO:0000256|ARBA:ARBA00004371}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}. 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; KZ505970; PKU42669.1; -; Genomic_DNA. 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:0005975; P:carbohydrate metabolic process; IEA:InterPro. 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 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR001093-2}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..558 FT /note="Beta-hexosaminidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014190499" FT DOMAIN 52..178 FT /note="Glycohydro_20b2" FT /evidence="ECO:0000259|Pfam:PF14845" FT DOMAIN 200..516 FT /note="Glyco_hydro_20" FT /evidence="ECO:0000259|Pfam:PF00728" FT ACT_SITE 355 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1" FT DISULFID 87..137 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" FT DISULFID 309..360 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" FT DISULFID 534..551 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" SQ SEQUENCE 558 AA; 62896 MW; DDC3972197437471 CRC64; MGLAGLLLGL FLVPAVLVST SLRHGVPPTE PEAPPELAEW ESVSGTVRED SLWPLPQWLR TSRRQLQLAP GRFQLVHGAG SSAGPGCGLL QDAFRRYYEY MFGQSRGRTW GRGPPGGLGG PELLELQVVI EAPDPGCNSY PHLASSEAYH LTVTEPVAIL KADEVWGALR GLETFSQLVH EDDYGSFLVN ESEIDDFPRF AHRGILLDTS RHYLPLKSIL TNLDAMAFNK FNVLHWHIVD DQSFPYQSIY FPELSDKGAY SYNHIYTPTD VRLVIEYARL RGIRVIPEFD TPGHTQSWGK GQKDLLTPCY SGKHPTGSFG PVNPILNTTY DFMTKFYKEI SNVFPDAYIH LGGDEVDFNC WKSNPDVREF MKQQGFGIDY AKLESYYIQK ILDIVSSNNK GYVVWQEVFD NKAQLKPDTV VQVWIGNNYA HELSSVTGAG FTAILSAPWY LDYISYGQDW KKYYSVEPLN FPGSEKQKKL LIGGEACLWG EFVDATNLTP RLWPRASAVG ERLWSSRNVT NLQDAYERLT NHRCRMLRRG IAAEPVFTGY CAHEARGQ //