ID   E3MZL2_CAERE            Unreviewed;       541 AA.
AC   E3MZL2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Glucosylceramidase {ECO:0000256|ARBA:ARBA00012658, ECO:0000256|RuleBase:RU361188};
DE            EC=3.2.1.45 {ECO:0000256|ARBA:ARBA00012658, ECO:0000256|RuleBase:RU361188};
GN   ORFNames=CRE_06915 {ECO:0000313|EMBL:EFP13061.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC         acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC         ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC         ChEBI:CHEBI:52639; EC=3.2.1.45;
CC         Evidence={ECO:0000256|RuleBase:RU361188};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC       {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
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DR   EMBL; DS268501; EFP13061.1; -; Genomic_DNA.
DR   RefSeq; XP_003098444.1; XM_003098396.1.
DR   AlphaFoldDB; E3MZL2; -.
DR   STRING; 31234.E3MZL2; -.
DR   EnsemblMetazoa; CRE06915.1; CRE06915.1; WBGene00067034.
DR   eggNOG; KOG2566; Eukaryota.
DR   HOGENOM; CLU_014379_1_2_1; -.
DR   InParanoid; E3MZL2; -.
DR   OMA; FGGIAWH; -.
DR   OrthoDB; 3473901at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR   PANTHER; PTHR11069:SF37; GLUCOSYLCERAMIDASE 1-RELATED; 1.
DR   Pfam; PF02055; Glyco_hydro_30; 1.
DR   Pfam; PF17189; Glyco_hydro_30C; 1.
DR   PRINTS; PR00843; GLHYDRLASE30.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361188};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361188};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sphingolipid metabolism {ECO:0000256|RuleBase:RU361188}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..541
FT                   /note="Glucosylceramidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003177780"
FT   DOMAIN          116..463
FT                   /note="Glycosyl hydrolase family 30 TIM-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF02055"
FT   DOMAIN          466..534
FT                   /note="Glycosyl hydrolase family 30 beta sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17189"
SQ   SEQUENCE   541 AA;  60270 MW;  39597666FE920CE4 CRC64;
     MKSRFRTIFS FIFFIIFCLG RSQTFHKKIL SNRAHFLAAN ADDCTSKSFK DGTVCVCSLD
     YCDEIPALDI TMGQAAVYMS SHAGARMHRD VIYATDAEPF GTLHLTIDSS KMYQTIQGFG
     STFSDASGAN LRSLPDKLAD TVIRQYFSES GLNLQFGRVP IASSDFSGRV YSYNDVSDDY
     MMQNFNLTKE DFQWKIPYIQ AAKKYNQNLK LFGAPWSAPG WMKTTKAMSG PGALSGKAGD
     NYHKAYTTYF VRFLEEYAKS GISFWALSTQ NQPTLGSDKK NKIQSTLFTA ETQRDFIKSD
     LGPALKGSNV GKDVKVLIMD DNRGNLPKWA DTVLNDRDAA PFVAGIGVHS YQDSESDKHL
     DETHKNHPNF FILGTEASEG GGAKDVSVDY GSWDRAEDTV SDILDDLNNW VVGWTERNLI
     LDAQGGPSWV SDFADAPIIA FPALAQFYKQ PMFYAIAHFS HFIKPGAVRI DHSLNVIELE
     VESSAFLNPD GSKVIVMVNK GSLVATEHTV VVQDTADNRN HYQFKLPHRS ITTLYIQTSN
     F
//