EGH1_YEAST
ID EGH1_YEAST Reviewed; 764 AA.
AC P40566; D6VVT7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ergosteryl-beta-glucosidase {ECO:0000303|PubMed:26116408};
DE EC=3.2.1.- {ECO:0000269|PubMed:26116408};
GN Name=EGH1 {ECO:0000303|PubMed:26116408}; OrderedLocusNames=YIR007W;
GN ORFNames=YIB7W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-594, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26116408; DOI=10.1093/glycob/cwv045;
RA Watanabe T., Tani M., Ishibashi Y., Endo I., Okino N., Ito M.;
RT "Ergosteryl-beta-glucosidase (Egh1) involved in sterylglucoside catabolism
RT and vacuole formation in Saccharomyces cerevisiae.";
RL Glycobiology 25:1079-1089(2015).
CC -!- FUNCTION: Ergosteryl beta-glucosidase involved in the ergosteryl beta-
CC glucoside (EG) catabolic pathway and vacuole formation via hydrolysis
CC of EG to generate glucose (PubMed:26116408). Is also able to hydrolyze
CC cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate
CC glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate
CC C6-NBD-ceramide (Cer) (PubMed:26116408). {ECO:0000269|PubMed:26116408}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ergosteryl 3-beta-D-glucoside + H2O = D-glucose + ergosterol;
CC Xref=Rhea:RHEA:24640, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16933, ChEBI:CHEBI:52973;
CC Evidence={ECO:0000269|PubMed:26116408};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26116408}.
CC Vacuole membrane {ECO:0000269|PubMed:26116408}; Peripheral membrane
CC protein {ECO:0000269|PubMed:26116408}. Note=Localizes in the cytosol
CC until the initial logarithmic phase, then targets to a yet unidentified
CC organelle with a granule structure in the middle logarithmic phase, and
CC finally localizes at the vacuole membranes in the stationary phase.
CC {ECO:0000269|PubMed:26116408}.
CC -!- DISRUPTION PHENOTYPE: Resulted in the accumulation of ergosteryl beta-
CC glucoside (EG) and fragmentation of vacuoles.
CC {ECO:0000269|PubMed:26116408}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z37996; CAA86077.1; -; Genomic_DNA.
DR EMBL; Z38062; CAA86209.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08553.1; -; Genomic_DNA.
DR PIR; S50878; S50878.
DR RefSeq; NP_012272.3; NM_001179529.3.
DR AlphaFoldDB; P40566; -.
DR SMR; P40566; -.
DR BioGRID; 34999; 60.
DR MINT; P40566; -.
DR STRING; 4932.YIR007W; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR iPTMnet; P40566; -.
DR MaxQB; P40566; -.
DR PaxDb; P40566; -.
DR PRIDE; P40566; -.
DR EnsemblFungi; YIR007W_mRNA; YIR007W; YIR007W.
DR GeneID; 854824; -.
DR KEGG; sce:YIR007W; -.
DR SGD; S000001446; EGH1.
DR VEuPathDB; FungiDB:YIR007W; -.
DR eggNOG; ENOG502QPU8; Eukaryota.
DR HOGENOM; CLU_009024_0_1_1; -.
DR InParanoid; P40566; -.
DR OMA; NEVVIGW; -.
DR BioCyc; MetaCyc:G3O-31428-MON; -.
DR BioCyc; YEAST:G3O-31428-MON; -.
DR BRENDA; 3.2.1.104; 984.
DR PRO; PR:P40566; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40566; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0050295; F:steryl-beta-glucosidase activity; IDA:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904462; P:ergosteryl 3-beta-D-glucoside catabolic process; IMP:SGD.
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 Cytoplasm; Glycosidase; Hydrolase; Membrane; Phosphoprotein;
KW Reference proteome; Vacuole.
FT CHAIN 1..764
FT /note="Ergosteryl-beta-glucosidase"
FT /id="PRO_0000184056"
FT REGION 588..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 515
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 764 AA; 86979 MW; 7D22AFE3E8E9FF02 CRC64;
MPAKIHISAD GQFCDKDGNE IQLRGVNLDP SVKIPAKPFL STHAPIENDT FFEDADKVSF
INHPLVLDDI EQHIIRLKSL GYNTIRLPFT WESLEHAGPG QYDFDYMDYI VEVLTRINSV
QQGMYIYLDP HQDVWSRFSG GSGAPLWTLY CAGFQPANFL ATDAAILHNY YIDPKTGREV
GKDEESYPKM VWPTNYFKLA CQTMFTLFFG GKQYAPKCTI NGENIQDYLQ GRFNDAIMTL
CARIKEKAPE LFESNCIIGL ESMNEPNCGY IGETNLDVIP KERNLKLGKT PTAFQSFMLG
EGIECTIDQY KRTFFGFSKG KPCTINPKGK KAWLSAEERD AIDAKYNWER NPEWKPDTCI
WKLHGVWEIQ NGKRPVLLKP NYFSQPDATV FINNHFVDYY TGIYNKFREF DQELFIIIQP
PVMKPPPNLQ NSKILDNRTI CACHFYDGMT LMYKTWNKRI GIDTYGLVNK KYSNPAFAVV
LGENNIRKCI RKQLSEMQKD AKSMLGKKVP VFFTEIGIPF DMDDKKAYIT NDYSSQTAAL
DALGFALEGS NLSYTLWCYC SINSHIWGDN WNNEDFSIWS PDDKPLYHDT RAKTPTPEPS
PASTVASVST STSKSGSSQP PSFIKPDNHL DLDSPSCTLK SDLSGFRALD AIMRPFPIQI
HGRFEFAEFN LCNKSYLLKL VGKTTPEQIT VPTYIFIPRH HFTPSRLSIR SSSGHYTYNT
DYQVLEWFHE PGHQFIEICA KSKSRPNTPG SDTSNDLPAE CVIS
