EGCR1_RHIO9
ID EGCR1_RHIO9 Reviewed; 683 AA.
AC I1BTD7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
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};
DE AltName: Full=Glucocerebrosidase {ECO:0000303|PubMed:22072709};
GN Name=ERC1 {ECO:0000303|PubMed:22072709};
GN ORFNames=RO3G_04172 {ECO:0000312|EMBL:EIE79467.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000312|Proteomes:UP000009138};
RN [1] {ECO:0000312|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000312|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-254 AND GLU-483.
RC STRAIN=NBRC 9364;
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).
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 -!- ACTIVITY REGULATION: Inhibited by metal cations Co(2+), Cu(2+), Ni(2+),
CC Pb(2+) and Zn(2+) (PubMed:22072709). Not inhibited by metal chelator
CC ethylenediaminetetraacetic acid (EDTA) (PubMed:22072709).
CC {ECO:0000269|PubMed:22072709}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:22072709};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {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; CH476733; EIE79467.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BTD7; -.
DR SMR; I1BTD7; -.
DR STRING; 936053.I1BTD7; -.
DR EnsemblFungi; EIE79467; EIE79467; RO3G_04172.
DR VEuPathDB; FungiDB:RO3G_04172; -.
DR eggNOG; ENOG502QPU8; Eukaryota.
DR InParanoid; I1BTD7; -.
DR OMA; HGRHFVD; -.
DR OrthoDB; 404674at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004348; F:glucosylceramidase activity; IDA:UniProtKB.
DR GO; GO:0043094; P:cellular metabolic compound salvage; ISS:UniProtKB.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR041036; GH5_C.
DR InterPro; IPR001547; Glyco_hydro_5.
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.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Membrane; Reference proteome.
FT CHAIN 1..683
FT /note="Glucosylceramidase"
FT /id="PRO_0000451756"
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 483
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT MUTAGEN 254
FT /note="E->Q: Abolishes glucosylceramidase activity."
FT /evidence="ECO:0000269|PubMed:22072709"
FT MUTAGEN 483
FT /note="E->Q: Abolishes glucosylceramidase activity."
FT /evidence="ECO:0000269|PubMed:22072709"
SQ SEQUENCE 683 AA; 78542 MW; 2F2840E0C17462B0 CRC64;
MTHPDRSAHD LNVPIQHSGR WFQDNLGRTL LLRGINVCGS SKLPTRPYPG STHLYDDILF
WDHRNVSFVN RPFPLEDAHE HFSRLSAWGL TLIRLLVPWE SIEHEGPGCY DEEYIDYLRQ
LIEMMPRYGI KCIIDPHQDT WSRFSGGSGA PGWTFEVAGL NIKHFKETGA AYVHNTNAVP
GDPLPMVWPT NYTKLASCTM FTLFFAGDTF APHRTYQSQS IQQFLNHHFI EAYRHLAERL
SDLEAVLAFE FMNEPHPGYI GLDHLDSFDP IMNLLFGDSP TPLQSFALGD GIPQTVDVYI
KSWPFPTKKS HDRVINASQT SAWFSGCVWK EHGVWTVDDQ GVPRLVNTHY FSKHPKTGEK
ISFYEDFYKP LVNRYVAAIQ SVKKEYYCLV EPLANEKPPV YNEHDHHHNV IFSPHWYDLD
SVFYKKFNAR MTHDVQCLQR GGNVFSATYF GKRGAKKNYR GQIKNIKEDG LLNMGEKPCI
MGEVGIPMDL NNKMAFEDDN YENHVHFMDA IIYALETNLI SFTLWNYDVF NDHEYGDHWN
GENFSIYSVK KSEEDYMRHD DGNSKLSKKH LYDGGRVLEA VLRPYAAKVA GTPVSAEFNI
DTLQYTFSFI PDCKGSTTTE IFVPYFHYGN KTIKTDVSFG RCSYIEEFQT LYHQYELNDP
LPKLVTITMG ILTTESANSC SVM
