ID A0A1V9XHE5_9ACAR Unreviewed; 386 AA.
AC A0A1V9XHE5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JUN-2023, entry version 20.
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=BIW11_10155 {ECO:0000313|EMBL:OQR72798.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR72798.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR72798.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR72798.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR72798.1}.
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DR EMBL; MNPL01011056; OQR72798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XHE5; -.
DR STRING; 418985.A0A1V9XHE5; -.
DR InParanoid; A0A1V9XHE5; -.
DR OrthoDB; 3473901at2759; -.
DR Proteomes; UP000192247; 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; 2.
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:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF02055; Glyco_hydro_30; 3.
DR PRINTS; PR00843; GLHYDRLASE30.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000192247};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sphingolipid metabolism {ECO:0000256|RuleBase:RU361188}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..386
FT /note="Glucosylceramidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012958168"
FT DOMAIN 99..187
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT DOMAIN 188..309
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT DOMAIN 311..382
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
SQ SEQUENCE 386 AA; 44020 MW; 363853A782C5C342 CRC64;
MVSRLLILAL LVLVASCLCE SDGHRELCYP KKFSYNFVVC VCNVTHCTDI GPTRPEEGHV
VMYQSLLNRL RFHKSRIHFG GTGTADLTLQ LGEKTVQKII GFKGAFTDAA GVNWLNLPEG
LRQRLLNSYY GPQGTGYSVG RIPMARCDFS TREYTYADKP DDVELGSFSL ADEDFHYKIP
MIKEAPKIKG EPGGPYYKTW AKYFVKFYQS YKENGVDIWG FTTQNEPASS YCPYTSQTMG
LTPDLERDFT NSDLGPALFN ITHGKIKLMA LDDNRYVLPW WANGLYRDPE AARYVAGLAV
HWYYDKHTSS DWDHAESYAF NILDDLRHAV PGWVDWNLFL DLQGGPNWAE NFLDAPIIVY
KENQAFHKQP MCYALAHFSK FLPLDQ
//
