GALC_XENTR
ID GALC_XENTR Reviewed; 678 AA.
AC Q0VA39;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) 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}.
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DR EMBL; BC121269; AAI21270.1; -; mRNA.
DR RefSeq; NP_001072270.1; NM_001078802.1.
DR AlphaFoldDB; Q0VA39; -.
DR SMR; Q0VA39; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR PaxDb; Q0VA39; -.
DR DNASU; 779723; -.
DR GeneID; 779723; -.
DR KEGG; xtr:779723; -.
DR CTD; 2581; -.
DR Xenbase; XB-GENE-1000107; galc.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR InParanoid; Q0VA39; -.
DR OrthoDB; 364933at2759; -.
DR Reactome; R-XTR-1660662; Glycosphingolipid metabolism.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000016608; Expressed in mesonephros and 15 other tissues.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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..678
FT /note="Galactocerebrosidase"
FT /id="PRO_0000370716"
FT ACT_SITE 190
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
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 388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 279..386
FT /evidence="ECO:0000250"
SQ SEQUENCE 678 AA; 75833 MW; 9A8DC79F7C3ED6CB CRC64;
MRTVLAGSRR APGCGEGMFI LWLVLLLFPG APAQYSVDDL GGLGRMFDGI GAISGGGATS
RLLVNYPEPQ RTEILDYLFK PNFGASLHIF KVEIGGDAQT TDGTEPSHMH YPDDQNYFRG
YEWWLMKEAK KRNPAIKLIG LPWAFPGWIG NGKNWPYDFP DVTAYYVVSW IIGAKQYHNL
DIDYIGIWNE RAYDIKYIKL LRYTLDKNNL EHVKIIASDN LWQPIAFHML QDPELLRVVD
VIGAHYPGTH AAQDAILTGK TLWASEDYST YNDEVGGGCW ARILNQNYVN GNMTSTISWN
MVASYYEQLP FGLEGLMTAK EPWSGNYVVS TPIWITAHTT QFTQPGWYYL KTVGHLDKGG
SYVALTDRLG NLTIVIETMS HNNSICIRPP LPDYNVSAQY ATFYLQGSFK NLQELQVWYS
SLDINNTKPV TFKKLSPLKV QNGSFTLQLG VNEVYTITTL LTGQKGSFPD PPESKPFPLK
YKDDFSVRNP PFSEAPYFAD QSGVFEYFTN TSDPGDHVFT FRQVLTQRPI TWASDANQAI
SVIGNYQWSN VTVTSDIYIE TPDTGGVFVA ARVDQGGSPT DRAKGIFFWV FADGTYKVTG
DLMGQTILCK GLAGVRARSW HTLTLHIDGT NAFGLLNGNP LWKEVVTGGP LNGWAAIGTS
CFEFAQFDNF MIEVKDSE
