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Database: UniProt
Entry: I3JW42_ORENI
LinkDB: I3JW42_ORENI
Original site: I3JW42_ORENI 
ID   I3JW42_ORENI            Unreviewed;       630 AA.
AC   I3JW42;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Galactocerebrosidase {ECO:0000256|ARBA:ARBA00019657};
DE            EC=3.2.1.46 {ECO:0000256|ARBA:ARBA00012657};
DE   AltName: Full=Galactosylceramidase {ECO:0000256|ARBA:ARBA00033098};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000013087.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000013087.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023982};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43413;
CC         Evidence={ECO:0000256|ARBA:ARBA00023982};
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:0000256|ARBA:ARBA00023423};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC         Evidence={ECO:0000256|ARBA:ARBA00023423};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family.
CC       {ECO:0000256|ARBA:ARBA00005637}.
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DR   AlphaFoldDB; I3JW42; -.
DR   Ensembl; ENSONIT00000013097.2; ENSONIP00000013087.2; ENSONIG00000010407.2.
DR   eggNOG; ENOG502QQ1Q; Eukaryota.
DR   GeneTree; ENSGT00390000003303; -.
DR   TreeFam; TF312985; -.
DR   Proteomes; UP000005207; Linkage group LG19.
DR   GO; GO:0004336; F:galactosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006683; P:galactosylceramide catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR049162; GH59_C.
DR   InterPro; IPR049161; GH59_cat.
DR   InterPro; IPR001286; Glyco_hydro_59.
DR   InterPro; IPR035394; Glyco_hydro_59_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR15172; GALACTOCEREBROSIDASE; 1.
DR   PANTHER; PTHR15172:SF1; GALACTOCEREBROSIDASE; 1.
DR   Pfam; PF02057; Glyco_hydro_59; 1.
DR   Pfam; PF21708; Glyco_hydro_59_C; 1.
DR   Pfam; PF17387; Glyco_hydro_59M; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..630
FT                   /note="Galactocerebrosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025543907"
FT   DOMAIN          40..331
FT                   /note="Glycosyl hydrolase family 59 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02057"
FT   DOMAIN          339..396
FT                   /note="Glycosyl hydrolase family 59 central"
FT                   /evidence="ECO:0000259|Pfam:PF17387"
FT   DOMAIN          455..627
FT                   /note="Glycosyl hydrolase family 59 C-terminal lectin"
FT                   /evidence="ECO:0000259|Pfam:PF21708"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
SQ   SEQUENCE   630 AA;  69540 MW;  94188ACD3D40FA62 CRC64;
     ALRMDCRESA LLVSVLFLAL DLCSAQNYVL SDDGGLGRVF DGIGGLSGGG ATSRLLVSYA
     EPYRSQILDF LFKPNFGASL HILKVEIGGD AQTTDGTEPS HMHYENDENY YRGYEWWLMK
     EAKKRNPNII LIGLPWAFPG WVGHGKNWPY DYPDVTATYV VNWILGAKQY HDLDIQYVGV
     STESMSLSPK VLRNMLDKVG LPGVGIIAAD GDWSVANSMI LDPYLKNSVD VIGAHYPGTT
     TITEALKTQK KLWSSEDYST FNNEVGGGCW ARILNQNYVN GQMTATISWN LVASYYEDLP
     FGRDGLMTAE EPWSGNYVVE SPIWITAHTT QFTQPGWTYL QTVGHLAQGG SYIALTDGKG
     NLTVVIETMT HNHSVCIRPP LPPFNVTSQN ATFQLKDGLF TLNLAEDEVY TLTTISTGSK
     GSYPDPPPSA PFPKVYKDDF DVRNPPFSEA PYFADQTGVF EYYINLTDPG PHVFTLRQVL
     TERPITWATD ADQTISVIGD YYWQNLTVTC DVFMEKMNAG GVFIAARVDK GGQSIRSAKG
     VFFWVFADGT YKVTNDLVGE TVLAEGQSGT EVYGWYTLSL TVKGQYASGS LNGYPLWKNA
     VVLTPKAGWA AIGTRSFELA QFDNFALVAE
//
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