ID   EXG_YARLI               Reviewed;         421 AA.
AC   Q12725; Q6C2T2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Glucan 1,3-beta-glucosidase;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase;
DE   Flags: Precursor;
GN   Name=EXG1; OrderedLocusNames=YALI0F05390g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX   PubMed=10029988;
RX   DOI=10.1002/(sici)1097-0061(19990130)15:2<91::aid-yea343>3.0.co;2-#;
RA   Esteban P.F., Vazquez de Aldana C.R., del Rey F.;
RT   "Cloning and characterization of 1,3-beta-glucanase-encoding genes from
RT   non-conventional yeasts.";
RL   Yeast 15:91-109(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; Z46872; CAA86952.1; -; Genomic_DNA.
DR   EMBL; CR382132; CAG77837.1; -; Genomic_DNA.
DR   RefSeq; XP_505030.1; XM_505030.1.
DR   AlphaFoldDB; Q12725; -.
DR   SMR; Q12725; -.
DR   STRING; 4952.CAG77837; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblFungi; CAG77837; CAG77837; YALI0_F05390g.
DR   GeneID; 2908269; -.
DR   KEGG; yli:YALI0F05390g; -.
DR   VEuPathDB; FungiDB:YALI0_F05390g; -.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   InParanoid; Q12725; -.
DR   OMA; DTHHYQV; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR   GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..421
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007888"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        321..347
FT                   /evidence="ECO:0000250"
FT   CONFLICT        333
FT                   /note="R -> S (in Ref. 1; CAA86952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  48275 MW;  2BB03184758252CC CRC64;
     MKLTKLVALA GAALASPIQL VPREGSFLGF NYGSEKVHGV NLGGWFVLEP FITPSLFEAF
     GNNDANVPVD EYHYTAWLGK EEAEKRLTDH WNTWITEYDI KAIAENYKLN LVRIPIGYWA
     FSLLPNDPYV QGQEAYLDRA LGWCRKYGVK AWVDVHGVPG SQNGFDNSGL RDHWDWPNAD
     NVQHSINVIN YIAGKYGAPE YNDIVVGIEL VNEPLGPAIG MEVIEKYFQE GFWTVRHAGS
     DTAVVIHDAF QEKNYFNNFM TTEQGFWNVV LDHHQYQVFS PGELARNIDQ HIAEVCNVGR
     QASTEYHWRI FGEWSAALTD CTHWLNGVGK GPRLDGSFPG SYYQRSCQGR GDIQTWSEQD
     KQESRRYVEA QLDAWEHGGD GWIYWTYKTE NALEWDFRRL VDNGIFPFPY WDRQFPNQCG
     F