ID Q7YTB2_9ASCI Unreviewed; 537 AA.
AC Q7YTB2;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN Name=Hexa-002 {ECO:0000313|EMBL:CAB3252627.1};
OS Phallusia mammillata.
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Ascidiidae; Phallusia.
OX NCBI_TaxID=59560 {ECO:0000313|EMBL:CAD57204.1};
RN [1] {ECO:0000313|EMBL:CAD57204.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:CAD57204.1};
RX PubMed=12828682; DOI=10.1046/j.1524-4725.2003.689.x;
RA Koyanagi R., Honegger T.G.;
RT "Molecular cloning and sequence analysis of an ascidian egg beta-N-
RT acetylhexosaminidase with a potential role in fertilization.";
RL Dev. Growth Differ. 45:209-218(2003).
RN [2] {ECO:0000313|EMBL:CAB3252627.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole embryo {ECO:0000313|EMBL:CAB3252627.1};
RA Neveu A P.;
RL Submitted (APR-2020) 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=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:ARBA00043767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941;
CC Evidence={ECO:0000256|ARBA:ARBA00043767};
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:ARBA00043827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969;
CC Evidence={ECO:0000256|ARBA:ARBA00043827};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR EMBL; LR785739; CAB3252627.1; -; mRNA.
DR EMBL; AJ518021; CAD57204.1; -; mRNA.
DR AlphaFoldDB; Q7YTB2; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
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 InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 2: Evidence at transcript level;
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..537
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033977528"
FT DOMAIN 40..156
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 178..495
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 334
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
FT DISULFID 72..116
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT DISULFID 288..339
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT DISULFID 513..530
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
SQ SEQUENCE 537 AA; 61038 MW; AD058C0845262A7B CRC64;
MKSVALFSLF LFCVGANANS QIKGEKVEIN VRELGSPGSV WPQPQHYSST TQTYAVVAEA
FQFVYSSTSH KCDLLTEAFK RYETLIYNNV ATIKLKYFPR DVASIKTLEV DLMSPCEDYP
SDHMKESYAL DVADKASLTS DTVWGILRGL ETFSQLLWAS DSNQVVVNKT NIIDYPRYAF
RGVMIDTARH YLPLNAILQT LDAMSYNKFN VLHWHIVDDQ SFPYVSDVYP DLSIKGAYDD
RTHIYTREDI AAVIEFARLR GIRVIPEFDS PGHSTSWGKG QPGLLTPCYS NGKPDGTFGP
INPTLNSTYT FVKNLFGDVK QVFHDNYIHL GGDEVQFNCW QSNPNITKWM SDKNITGDYS
KLEQVYIQNV IDISETIGYS YIVWQEVIDN GVKVQSDTVV EVWKNNHPDQ EVAKVTAMGL
RAIVSAPWYL NIISYGQDWH KYYQYDPSNF NGTAEQKALV MGGEACIWGE YVDATNLSPR
LWPRASAVAE RLWSAESVND VDAAYPRLDQ QRCRMIRRGI PAQPLYIGFC PHEWKNY
//
