GALC_XENLA
ID GALC_XENLA Reviewed; 677 AA.
AC Q498K0; Q66IP0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Galactocerebrosidase {ECO:0000250|UniProtKB:P54803};
DE Short=GALCERase;
DE EC=3.2.1.46 {ECO:0000250|UniProtKB:P54803};
DE AltName: Full=Galactosylceramidase;
DE Flags: Precursor;
GN Name=galc {ECO:0000250|UniProtKB:P54803};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the galactose ester bonds of glycolipids such as
CC galactosylceramide and galactosylsphingosine.
CC {ECO:0000250|UniProtKB:P54803}.
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:P54803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000250|UniProtKB:P54803};
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:P54803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-galactosylceramide + H2O = an N-acyl-sphingoid base + D-
CC galactose; Xref=Rhea:RHEA:43412, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36498, ChEBI:CHEBI:83273;
CC Evidence={ECO:0000250|UniProtKB:P54818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43413;
CC Evidence={ECO:0000250|UniProtKB:P54818};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC081270; AAH81270.1; -; mRNA.
DR EMBL; BC100187; AAI00188.1; ALT_INIT; mRNA.
DR RefSeq; XP_018085879.1; XM_018230390.1.
DR AlphaFoldDB; Q498K0; -.
DR SMR; Q498K0; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR GeneID; 446948; -.
DR KEGG; xla:446948; -.
DR CTD; 446948; -.
DR Xenbase; XB-GENE-1000113; galc.L.
DR OMA; VASDNLW; -.
DR OrthoDB; 364933at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 446948; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0006683; P:galactosylceramide catabolic process; ISS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001286; Glyco_hydro_59.
DR InterPro; IPR035394; Glyco_hydro_59_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR15172; PTHR15172; 1.
DR Pfam; PF02057; Glyco_hydro_59; 1.
DR Pfam; PF17387; Glyco_hydro_59M; 1.
DR PRINTS; PR00850; GLHYDRLASE59.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Reference proteome; Signal;
KW Sphingolipid metabolism.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..677
FT /note="Galactocerebrosidase"
FT /id="PRO_0000370715"
FT ACT_SITE 190
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..385
FT /evidence="ECO:0000250"
SQ SEQUENCE 677 AA; 75061 MW; 5ACED0C555AF7A04 CRC64;
MGTVPAGSRR APGCGEGMFI LCLALLLAPG APAQYSVDDF GGLGRMFDGI GAISGGGATS
RLLVNYPEPQ RTEILDYLFK PNFGASLHIF KVEIGGDAQT TDGTEPSHMH YPDDQNYFRG
YEWWLMKEAK KRNPAIKLIG LPWAFPGWIG YGKNWPYDFP DVTAYYVVSW IIGAKQYHNL
DIDYIGIWNE RAYDIKYIKV LRHTLDRLGL TNVGIIAADG DWGIAHDVLI DPYLNEAVQV
IGAHYPGTHA AQDAIQTGKT LWASEDYSTY NDEVGGGCWA RILNQNYVNG NMTSTISWNM
VASYYEQLPF GLEGLMTAKE PWSGNYVVST PIWITAHTTQ FTQPGWYYLR TVGHLDKGGS
YVALTDRLGN LTVIIETMSH NNSICIRPPL PEYNVSAQNA TFYLQGSFQN LQELQVWYSN
LDINNTKPVT FKKLTPVKVQ NGSFTLQLGV NEVYTVTTLL TGQKGSFPDP PKSKPFPLKY
KDDFSVRNPP FSEAPYFADQ SGVFEYFTNT SDPGDHVFTF RQVLTQRPIT WASDANQAIS
VIGNYQWSNI TVTCDIYIET VETGGVFVAA RVDQGGSPTD RAKGIFFWVF ADGTYKVTGD
LIGEIVLCKG LAGVRARSWH TLTLHVDGTN ASGLLNGSPL WKEVVTGGPL HGWAAIGTSS
FEFTQFDNFM IEAKDPE
