ID   EGCR1_ASPFM             Reviewed;         759 AA.
AC   H1AE13;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Glucosylceramidase {ECO:0000303|PubMed:22072709};
DE            EC=3.2.1.45 {ECO:0000269|PubMed:22072709};
DE   AltName: Full=Endoglycoceramidase-related protein 1 {ECO:0000303|PubMed:22072709};
DE            Short=EGCrP1 {ECO:0000303|PubMed:22072709};
GN   Name=egc1 {ECO:0000303|PubMed:22072709};
GN   ORFNames=CDV57_02266 {ECO:0000312|EMBL:OXN27561.1};
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128 {ECO:0000312|EMBL:BAL46041.1};
RN   [1] {ECO:0000312|EMBL:BAL46041.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=NBRC 33022 {ECO:0000312|EMBL:BAL46041.1};
RX   PubMed=22072709; DOI=10.1074/jbc.m111.311340;
RA   Ishibashi Y., Ikeda K., Sakaguchi K., Okino N., Taguchi R., Ito M.;
RT   "Quality control of fungus-specific glucosylceramide in Cryptococcus
RT   neoformans by endoglycoceramidase-related protein 1 (EGCrP1).";
RL   J. Biol. Chem. 287:368-381(2012).
RN   [2] {ECO:0000312|Proteomes:UP000215142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 270 {ECO:0000312|Proteomes:UP000215142};
RX   PubMed=31891387; DOI=10.1093/jac/dkz534;
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Folch B., Martineau C.,
RA   Moreira S., Doucet N., De Repentigny L., Dufresne S.F.;
RT   "Prevalence and mechanisms of azole resistance in clinical isolates of
RT   Aspergillus section Fumigati species in a Canadian tertiary care centre,
RT   2000 to 2013.";
RL   J. Antimicrob. Chemother. 75:849-858(2020).
CC   -!- FUNCTION: Specifically hydrolyzes the glucosidic linkage in
CC       glucosylceramide (PubMed:22072709). May prevent accumulation of
CC       aberrent glucosylceramide containing immature ceramide (By similarity).
CC       {ECO:0000250|UniProtKB:H1AE12, ECO:0000269|PubMed:22072709}.
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:0000269|PubMed:22072709};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC         Evidence={ECO:0000269|PubMed:22072709};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB669901; BAL46041.1; -; mRNA.
DR   EMBL; NKHT01000047; OXN27561.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1AE13; -.
DR   SMR; H1AE13; -.
DR   OMA; NEVVIGW; -.
DR   Proteomes; UP000215142; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Membrane.
FT   CHAIN           1..759
FT                   /note="Glucosylceramidase"
FT                   /id="PRO_0000451754"
FT   REGION          576..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        247
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        497
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   759 AA;  86064 MW;  5CE99981A49DB31C CRC64;
     MGVLRLRVDG QTFRDPDNRE ITLRGINVAG EAKYPKKPDI PSYVSDGFFD ADNVSFVGRP
     FSLDDAHTHF SRLRKWGYNT IRYVFTWEAI EHEGPGKYDD EWISFTIEVL RIAKQYGFYV
     FLDPHQDVWS RLSGGSGAPA WTLYAAGFDP RGFKKTEAAL VQNTFDDPAE FPKMIWSTNY
     TRLVSQTMFT LFYGGRDFAP KAIIDGINIQ DYLQGHFIAA CRYFAQKIHE AGDIENEVVI
     GWESMNEPNR GLIGVQDISV IPPEQQLQLG TSPTAFQGML TGSGRACEES TWAFGGFGPY
     QTGRELVDPE GETAWLPADY DDTRYGWVRD PGWKLGECLW AQHGVWDPSS DKLLRKDYFA
     KNPQTGEPLN YDKFTNTYFM EHYRAYRDAL RSVWPEAIIF CQPPVMEVPP DLKGTVDDDP
     NMVHAVHYYD GITLLTKHWN RLYNVDVIGV LRGKYLTPAF AVKIGETAIR NCLRDQLKFL
     RDESLRYMGT HPLIFTEIGI PFDMDDRHAY KTGDYSGQVS AMDANHFAIE GSTANGFTLW
     LYTTSNNHEW GDNWNGEDLS IYSVDDLELP SGKLLAFENE SQRDPQSPAY SESQRNTESY
     RVGPRDLKQA LQAPSISSEI SQSSQDKLGF RAAEAWVRPS PIITNGQILQ YGFDLKSCVF
     SMRLLGEKKG LGQEAATEIF LPDFHFPDTH TVVAVSAGEW TIDYPEIHSV KFQRLRWWHP
     EGDHNIKIQG VKRKPGDPTV SGEELSYLEQ CQGGGCSVM