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Database: UniProt/TrEMBL
Entry: B0WDK1_CULQU
LinkDB: B0WDK1_CULQU
Original site: B0WDK1_CULQU 
ID   B0WDK1_CULQU            Unreviewed;       539 AA.
AC   B0WDK1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   Name=6036791 {ECO:0000313|EnsemblMetazoa:CPIJ005343-PA};
GN   ORFNames=CpipJ_CPIJ005343 {ECO:0000313|EMBL:EDS44610.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS44610.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS44610.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ005343-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ005343-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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; DS231898; EDS44610.1; -; Genomic_DNA.
DR   RefSeq; XP_001846785.1; XM_001846733.1.
DR   AlphaFoldDB; B0WDK1; -.
DR   STRING; 7176.B0WDK1; -.
DR   EnsemblMetazoa; CPIJ005343-RA; CPIJ005343-PA; CPIJ005343.
DR   KEGG; cqu:CpipJ_CPIJ005343; -.
DR   VEuPathDB; VectorBase:CPIJ005343; -.
DR   eggNOG; KOG2566; Eukaryota.
DR   HOGENOM; CLU_014379_1_2_1; -.
DR   InParanoid; B0WDK1; -.
DR   OMA; GLMWNFA; -.
DR   Proteomes; UP000002320; 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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR   PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 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:UP000002320};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sphingolipid metabolism {ECO:0000256|RuleBase:RU361188}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..539
FT                   /note="Glucosylceramidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011407885"
FT   DOMAIN          120..472
FT                   /note="Glycosyl hydrolase family 30 TIM-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF02055"
FT   DOMAIN          475..536
FT                   /note="Glycosyl hydrolase family 30 beta sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17189"
SQ   SEQUENCE   539 AA;  60502 MW;  09BC442FA951BEF3 CRC64;
     MPHLNLIAAC ALLWAAGSAS LTAGASLPCA LRQYPSGSVC VCNATYCDTL EFEEPKVAGE
     FVLVSSGRDG ARFREARGRF VNASRVEFLP VVMRTNGRRV VRATREVTVT VNRGRKFQRV
     VGFGGAFTGA VAYNLGLLKP ELRKSLYRSY YSKKVGIGYN LMRIPIGGCD FDLKPWAYNE
     VPVDDVGLSN FTKLDDRDVV KIAQIKELME VAENRNVKIM GAAWSPPRWM KSNNDWSGSS
     RLKTEYFQTW ADYHIRYLQL MKDAGLDYWA ISTGNEPMNA VIGFLFIRFM SLGWTAIEQG
     KWVGENLGPA LRNSAFKDVK LFAGDDQRYT FPWWFSQMDQ GHANATQYLD GLAVHWYWDG
     VTPAALLDQA AKQYPDKLLF NTEASLGDKP FQTHGPILGS WDRAESYITY ILQDLQHSVN
     GWIDWNLLLN EIGGPNYANN YVETAVVVNA TSGEEVYKQP IFYGLGHFSR FITEGSMRLE
     TISSDSGVIV VGFERSDKLT TLVFYNKKST PCELTIKDPD RGTTQLRLEP KSVHSILYA
//
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