GBA3_PONAB
ID GBA3_PONAB Reviewed; 469 AA.
AC Q5RF65;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytosolic beta-glucosidase {ECO:0000305};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q9H227};
DE AltName: Full=Cytosolic galactosylceramidase {ECO:0000305};
DE EC=3.2.1.46 {ECO:0000250|UniProtKB:Q9H227};
DE AltName: Full=Cytosolic glucosylceramidase {ECO:0000305};
DE EC=3.2.1.45 {ECO:0000250|UniProtKB:Q9H227};
DE AltName: Full=Cytosolic glycosylceramidase {ECO:0000250|UniProtKB:Q9H227};
DE Short=Cytosolic GCase {ECO:0000250|UniProtKB:Q9H227};
GN Name=GBA3 {ECO:0000250|UniProtKB:Q9H227};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Neutral cytosolic beta-glycosidase with a broad substrate
CC specificity that could play a role in the catabolism of
CC glycosylceramides. Has a significant glucosylceramidase activity in
CC vitro. However, that activity is relatively low and its significance in
CC vivo is not clear. Hydrolyzes galactosylceramides/GalCers,
CC glucosylsphingosines/GlcSphs and galactosylsphingosines/GalSphs.
CC However, the in vivo relevance of these activities is unclear. It can
CC also hydrolyze a broad variety of dietary glycosides including
CC phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro
CC and could therefore play a role in the metabolism of xenobiotics.
CC Possesses transxylosylase activity in vitro using xylosylated
CC ceramides/XylCers (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-
CC enine) as xylosyl donors and cholesterol as acceptor. Could also play a
CC role in the catabolism of cytosolic sialyl free N-glycans.
CC {ECO:0000250|UniProtKB:Q9H227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639; EC=3.2.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an
CC N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390,
CC ChEBI:CHEBI:52639; EC=3.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1)-sphing-4-enine + H2O = D-glucose +
CC sphing-4-enine; Xref=Rhea:RHEA:59288, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:83992;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59289;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1)-N-octadecanoylsphing-4-enine + H2O =
CC D-glucose + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:59284,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:72961,
CC ChEBI:CHEBI:84719; Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59285;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1)-sphing-4-enine + H2O = D-galactose +
CC sphing-4-enine; Xref=Rhea:RHEA:43908, ChEBI:CHEBI:4139,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:57934;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1')-N-octadecanoylsphing-4-enine + H2O
CC = D-galactose + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:59292,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:72961,
CC ChEBI:CHEBI:84720; Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59293;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine + cholesterol =
CC an N-acylsphing-4-enine + cholesteryl 3-beta-D-xyloside;
CC Xref=Rhea:RHEA:70239, ChEBI:CHEBI:16113, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:189067, ChEBI:CHEBI:189068;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70240;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70241;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9H227}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q9H227}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
CC subfamily. {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; CR857296; CAH89592.1; -; mRNA.
DR RefSeq; NP_001124705.1; NM_001131233.1.
DR AlphaFoldDB; Q5RF65; -.
DR SMR; Q5RF65; -.
DR STRING; 9601.ENSPPYP00000016355; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR Ensembl; ENSPPYT00000017020; ENSPPYP00000016355; ENSPPYG00000014639.
DR GeneID; 100171553; -.
DR KEGG; pon:100171553; -.
DR CTD; 57733; -.
DR eggNOG; KOG0626; Eukaryota.
DR GeneTree; ENSGT00940000160460; -.
DR HOGENOM; CLU_001859_1_3_1; -.
DR InParanoid; Q5RF65; -.
DR OMA; DWVYVVP; -.
DR OrthoDB; 408001at2759; -.
DR TreeFam; TF314803; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0004348; F:glucosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0017042; F:glycosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901805; P:beta-glucoside catabolic process; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006683; P:galactosylceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0006680; P:glucosylceramide catabolic process; ISS:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycosidase; Hydrolase; Lipid metabolism; Reference proteome.
FT CHAIN 1..469
FT /note="Cytosolic beta-glucosidase"
FT /id="PRO_0000063909"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 424..425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 53747 MW; EC6DFA9543EA6843 CRC64;
MAFPVGFGWA AATAAYQVEG GWDADGKGPC VWDTFTHQGG ERVFKNQTGD VACGSYTLWE
EDLKCIKQLG LTHYRFSLSW SRLLPDGTTG FINQKGIDYY NKIIDDLLKN GVTPIVTLYH
FDLPQALEDQ GGWLSEAIIE SFDKYAQFCF STFGDRVKKW ITINEANVLS VMSYDLGMFP
PGIPHFGTGG YQAAHNLIKA HARSWHSYNS LFRKEQKGMV SLSLFAVWLE PADPNSVSDQ
EAAKRAITFH LDLFAKPIFI DGDYPEIVKS QIASMSQKQG YPSSRLPEFT EEEKKMIKGT
ADFFAVQYYT TRLIKYQENK KGELGILQDA EIEFFPDPSW KNVDWIYVVP WGVRKLLKYI
KDTYNNPVIY ITENGFPQSD PAPLDDTQRW EYFRQTFQEL FKAIQLDKVN LQVYCAWSLL
DNFEWNQGYS SRFGLFHVDF EDPARPRVPY TSAKEYAKVI RNNGLEAHL
