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Database: UniProt
Entry: W5UDI8_ICTPU
LinkDB: W5UDI8_ICTPU
Original site: W5UDI8_ICTPU 
ID   W5UDI8_ICTPU            Unreviewed;       659 AA.
AC   W5UDI8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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};
GN   Name=galc {ECO:0000313|EMBL:AHH39940.1};
GN   Synonyms=galca {ECO:0000313|RefSeq:XP_017312088.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH39940.1};
RN   [1] {ECO:0000313|EMBL:AHH39940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed {ECO:0000313|EMBL:AHH39940.1};
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
RN   [2] {ECO:0000313|RefSeq:XP_017312088.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017312088.1};
RG   RefSeq;
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   EMBL; JT412651; AHH39940.1; -; mRNA.
DR   RefSeq; XP_017312088.1; XM_017456599.3.
DR   STRING; 7998.ENSIPUP00000008923; -.
DR   Ensembl; ENSIPUT00000009312; ENSIPUP00000008923; ENSIPUG00000006035.
DR   GeneID; 108258153; -.
DR   KEGG; ipu:108258153; -.
DR   CTD; 449649; -.
DR   OMA; HEAWDEN; -.
DR   OrthoDB; 5487508at2759; -.
DR   Proteomes; UP000221080; Chromosome 25.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
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   PRINTS; PR00850; GLHYDRLASE59.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   2: Evidence at transcript level;
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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..659
FT                   /note="Galactocerebrosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013540188"
FT   DOMAIN          33..326
FT                   /note="Glycosyl hydrolase family 59 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02057"
FT   DOMAIN          334..449
FT                   /note="Glycosyl hydrolase family 59 central"
FT                   /evidence="ECO:0000259|Pfam:PF17387"
FT   DOMAIN          485..658
FT                   /note="Glycosyl hydrolase family 59 C-terminal lectin"
FT                   /evidence="ECO:0000259|Pfam:PF21708"
FT   ACT_SITE        176
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
SQ   SEQUENCE   659 AA;  73769 MW;  57001183FAAEB49A CRC64;
     MNSYVVLFLF SFIRLCVTEK YVLDDRLGLG RQFDGIGGLS GGGATSRLLI NYKEPYRSQI
     LDYLFKPNFG ASLHILKVEI GGDSQTTDGT EPSHMHNETD ENYFRGYEWW LMKEAKQRNP
     NITLIGLPWA FPGWVGNGSK WPYNFPDITA NYVVSWVIGA KQYHGLDIDY IGVWNERTFD
     SKYIQVLRNK LDQADLPNIG IIAADGNWDI SNAMLVDPYL NDAVEIIGVH YPGTMTVKEA
     LLTDKKLWSS EDYSTFNNDI GAGCWARILN QNYVNGRMTS TISWNLIASY YEDLSFGRDG
     LMTAEEPWSG NYVAETPIWI TAHTTQFAQP GWTYLQTIGN LTRGGSYVAL TDGQGNLTII
     IETMTHNHSQ CIRPPLPPFS VSPQEATFQL KGSFAAVNGL QLWYSKLDFN TKKDVLFKKA
     DPIKVSNGCF TLKLDVDEIY TITTVTTGQK GLYPNPPDSA SFPKKYFDDF NVQNPPFSEA
     PYFADQTGVF EYFTNLMDPG PHNLTLRQVV NQQPVSWGYD ADQTISIIGD HGWQDVSVSC
     DIYLETEDGG VFVAARVDQS GESVRRAKGV FYWVFANGTY KVTNDIGGEK VLAEGLSGTR
     PGIWHTLTLI VKGNYAFGML NGFPLWKNAV VLQPKNGWAA IGTSSFEFAQ FDNFLVDAD
//
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