ID H2NLZ1_PONAB Unreviewed; 589 AA.
AC H2NLZ1; A0A2J8W5I8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 59.
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|Ensembl:ENSPPYP00000006875.3};
GN ORFNames=CR201_G0012987 {ECO:0000313|EMBL:PNJ65039.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000006875.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000006875.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ65039.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ65039.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000006875.3}
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 EMBL; NDHI03003399; PNJ65039.1; -; Genomic_DNA.
DR Ensembl; ENSPPYT00000007145.3; ENSPPYP00000006875.3; ENSPPYG00000006046.3.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR GeneTree; ENSGT00390000003303; -.
DR HOGENOM; CLU_015456_2_0_1; -.
DR TreeFam; TF312985; -.
DR Proteomes; UP000001595; Chromosome 14.
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:UP000001595};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT DOMAIN 10..293
FT /note="Glycosyl hydrolase family 59 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02057"
FT DOMAIN 301..416
FT /note="Glycosyl hydrolase family 59 central"
FT /evidence="ECO:0000259|Pfam:PF17387"
FT DOMAIN 453..581
FT /note="Glycosyl hydrolase family 59 C-terminal lectin"
FT /evidence="ECO:0000259|Pfam:PF21708"
FT ACT_SITE 142
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR601286-50"
SQ SEQUENCE 589 AA; 67165 MW; 0BFA8993F4302B76 CRC64;
MGFMVADLWA TSRLLVNYPE PYRSQILDYL FKPNFGASLH ILKVEIGGDG QTTDGTEPSH
MHYALDENYF RGYEWWLMKE AKKRNPNITL IGLPWSFPGW LGKGFNWPYV NLQLTAYYVV
TWIVGAKRYH DLDIDYIGIW NERSYNANYI KILRKMLNYQ GLQRVKIIAS DNLWESISAS
MLLDAELFKV VDVIGAHYPG THSAKDAKLT GKKLWSSEDF STLNSDTGAG CWGRILNQNY
INGYMTSTIA WNLVASYYEQ LPYGRCGLMT AQEPWSGHYV VDSPVWVSAH TTQFTQPGWY
YLKTVGHLEK GGSYVALTDG LGNLTIIIET MSHKHSKCIR PFLPYFNVSQ QFATFVLKGS
FSEIPELQVW YTKLGKTSER FLFKQLDSLW LLDSDGSFTL NLHEDELFTL TTLTTGRKGS
YPLPPKSQPF PSTYKDDFNV DYPFFSEAPN FADQTGVFEY FTNIEDPGEH HFTLRQVLNQ
RPITWAADAS NTISIIGDYN WTNLTIKCDV YIETPDTGGV FIAGRVNKGG ILIRSARGIF
FWIFANGSYR VTGDLAGWII YALGRVEVTA KKWYTLTLTI KVAGRRKKT
//
