ID H2T8L4_TAKRU Unreviewed; 739 AA.
AC H2T8L4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 57.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000021004.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000021004.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000021004.3}
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; H2T8L4; -.
DR Ensembl; ENSTRUT00000021091.3; ENSTRUP00000021004.3; ENSTRUG00000008387.3.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR GeneTree; ENSGT00390000003303; -.
DR HOGENOM; CLU_015456_2_0_1; -.
DR InParanoid; H2T8L4; -.
DR OMA; KYPKNGW; -.
DR TreeFam; TF312985; -.
DR Proteomes; UP000005226; Chromosome 2.
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 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:UP000005226};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT DOMAIN 110..404
FT /note="Glycosyl hydrolase family 59 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02057"
FT DOMAIN 412..527
FT /note="Glycosyl hydrolase family 59 central"
FT /evidence="ECO:0000259|Pfam:PF17387"
FT DOMAIN 563..736
FT /note="Glycosyl hydrolase family 59 C-terminal lectin"
FT /evidence="ECO:0000259|Pfam:PF21708"
FT ACT_SITE 253
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
SQ SEQUENCE 739 AA; 83411 MW; 059C49281C45D260 CRC64;
MIHHKYSLFP VLIFKVKNPS CSHSWIQSWT SEERGKQKQG PNGHFGGPAL RCCWAGGTNA
DEIRESRPFP LKRRLPVSRD FQRRLINRIS FTLWLHAYYL SDKAGLGRVF DGIGGLSGGG
ATSRLLVNYA EPYRSQILDY LFKPNFGASL HILKVEIGGD AQSTDGTEPS HMHYEADENY
FRGYEWWLMK EAKKRNPNIT LIGLPWAFPG WVGHGNDWPY DFPDITAAYV VNWIIGAKQY
HDLDIQYIGI WNERSFDIKY IKLLRYTLDK SGLEEVKIIA SDNLWQPITR SLLLDAELHR
AVDIIGAHYP GTNTVMEALE TRKTLWSSED YSTFNDDVGG GCWARILNQN YVNGFMTATI
SWNLVASYYD NLPFSRDGLM TAEEPWSGNY VVESPIWITA HHTQFTQPGW TYLQTVGHLA
QGGSYVALTD GKGNLTIVIE TMTHDHSVCI RPPLPAFNVT SQTAMFQLEG SFASISEVQV
WRSHFGFKSK KPSFFERLTP LKLVDGFFSL HLMEDEVYTL TTLKVGQKGS YPSPPASSPF
PKVYKDDFNV RHPSFSEAPY FADQTGVFEY FMNLSDPGPH LYTLRQVITE RPVTWVADAD
QTISVIGDYQ WQNLTVTCDV FMETATTGGV FLAARVDRGG QAVRSTRGVF FWLFADGTYR
VTNDLAGQTV LAEGESGTRA YRWYTLTLTV QGQYASGQLN GYQLWSNAVV LTPKNGWVAI
GTRSFESNQF DNIAIVAKG
//
