GALC_CAEEL
ID GALC_CAEEL Reviewed; 645 AA.
AC Q95QT2;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative galactocerebrosidase;
DE Short=GALCERase;
DE EC=3.2.1.46;
DE AltName: Full=Galactocerebroside beta-galactosidase;
DE AltName: Full=Galactosylceramidase;
DE AltName: Full=Galactosylceramide beta-galactosidase;
DE Flags: Precursor;
GN ORFNames=C29E4.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Hydrolyzes the galactose ester bonds of galactosylceramide,
CC galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family. {ECO:0000305}.
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DR EMBL; FO080706; CCD66013.2; -; Genomic_DNA.
DR RefSeq; NP_498726.3; NM_066325.3.
DR AlphaFoldDB; Q95QT2; -.
DR SMR; Q95QT2; -.
DR STRING; 6239.C29E4.10; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR EPD; Q95QT2; -.
DR PaxDb; Q95QT2; -.
DR PeptideAtlas; Q95QT2; -.
DR PRIDE; Q95QT2; -.
DR EnsemblMetazoa; C29E4.10.1; C29E4.10.1; WBGene00016207.
DR GeneID; 183002; -.
DR KEGG; cel:CELE_C29E4.10; -.
DR UCSC; C29E4.10; c. elegans.
DR CTD; 183002; -.
DR WormBase; C29E4.10; CE47094; WBGene00016207; -.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR GeneTree; ENSGT00390000003303; -.
DR HOGENOM; CLU_508307_0_0_1; -.
DR InParanoid; Q95QT2; -.
DR OMA; WHLMSAF; -.
DR OrthoDB; 364933at2759; -.
DR PhylomeDB; Q95QT2; -.
DR Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR PRO; PR:Q95QT2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016207; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004336; F:galactosylceramidase activity; IBA:GO_Central.
DR GO; GO:0006683; P:galactosylceramide catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Signal; Sphingolipid metabolism.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..645
FT /note="Putative galactocerebrosidase"
FT /id="PRO_0000012233"
FT ACT_SITE 172
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
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 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 261..365
FT /evidence="ECO:0000250"
SQ SEQUENCE 645 AA; 73805 MW; BE060A32F3A33304 CRC64;
MFSIFIKIIL ILPSIATKTN NIDIKSWRSA QTFDGFGAVS GGGATSKLLF TYFSEKSDRK
QVLESLFNKD NGLQLLKVEM GGDDQSTEGT ESSHESEKGK ISKNNYEFQL ISEVREINPT
IPICVLPWAF PGWIGNTPYD NVTETAEYVV NWLKIGRDTW NFDTFCVGVW NERNFSESYV
KELRKILNLN GFNETLIVAG EGFRMDDSYS RLLDKRFINE YDIIGVHYPG GRIPENVQKS
GKVIWASEDY STDNRDTGEG CMARTMNWNF INGNITGMIS WHLMSAFYPQ LPWYRCGLAR
IDENKFQTEK AFHVLKYITS HVKRGWKILR ESSGRFDGGG TYVTYTNGKD STIFVETMSY
KKSLCEYSSP RPYHVKPSQL IRFKFSEIPS FQGLNMSLNF GPSKFFSKSV NSTITILLPV
NSFGILTTLP VSTPKRVTIK TPLVPLNYHD DFENYEFDEE PKFWMPQKGS WVVRNGRAVQ
KVTRPSISWC TSHIRTPYAV MAYRKKNSIL NAEVNIPKHS TAKSIILGIR SNCSGCDIEV
INCRGIFVEI EFSNKKVTIF SDFVDRSIIA EFKARRKVEF GKFYKFSIHL LDSHLFIKFG
NHHVMTSVEI PEEQLNKTNN DTLFVIGTGN FGISEWDNIS TDYFH
