ID   EXG1_SCHPO              Reviewed;         407 AA.
AC   Q9URU6; P78778;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Glucan 1,3-beta-glucosidase 1;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase;
DE   Flags: Precursor;
GN   Name=exg1; ORFNames=SPBC1105.05;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-407.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. It could also function
CC       biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAB50968.1; -; Genomic_DNA.
DR   EMBL; D89127; BAA13789.1; -; mRNA.
DR   PIR; T39282; T39282.
DR   PIR; T42370; T42370.
DR   RefSeq; NP_596461.1; NM_001022380.2.
DR   AlphaFoldDB; Q9URU6; -.
DR   SMR; Q9URU6; -.
DR   BioGRID; 276537; 21.
DR   STRING; 4896.SPBC1105.05.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   MaxQB; Q9URU6; -.
DR   PaxDb; Q9URU6; -.
DR   EnsemblFungi; SPBC1105.05.1; SPBC1105.05.1:pep; SPBC1105.05.
DR   GeneID; 2539993; -.
DR   KEGG; spo:SPBC1105.05; -.
DR   PomBase; SPBC1105.05; exg1.
DR   VEuPathDB; FungiDB:SPBC1105.05; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   InParanoid; Q9URU6; -.
DR   OMA; CWKTEST; -.
DR   PhylomeDB; Q9URU6; -.
DR   PRO; PR:Q9URU6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0000935; C:division septum; IDA:PomBase.
DR   GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IDA:PomBase.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
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; IDA:PomBase.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IGI:PomBase.
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   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..407
FT                   /note="Glucan 1,3-beta-glucosidase 1"
FT                   /id="PRO_0000007887"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        312
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        295..406
FT                   /evidence="ECO:0000250"
FT   CONFLICT        178
FT                   /note="Q -> E (in Ref. 2; BAA13789)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  45506 MW;  4F2C717A4C65ECF9 CRC64;
     MLSFTSVFSF FLHALLLKTA FSYVIKRNNP VFDYTSEKVR GVNIGGWLVL ENWITPQLFT
     QFSSMSNPPT DEWGFCEVLG ADEAASQLAA HYSSFYTESD FATIASWGVN VLRIPIGYWA
     FNVVDGEPYV QGQEYWLDQA LTWAEQYGLK VWIDLHGVPG SQNGFENSGK TGSIGWQQND
     TVTRTLDIIT YVANKYTQSQ YASVVIGIET VNEPLGYGLD MDQLKQYDLD AYNIVNPLSS
     SVATIIHDAY VDLSIWDYGV VSPSSYNLVM DVHRYQLYES DECSKTLDDH LSDVCSIGDS
     IASSPYITVT GEWSGTLADC TIFEEGVDSS TFIGPNSGDI STWTDEYKGA VRLFIETQLD
     QFERGAGWIY WTAKTGGPSP TWDMGLLIEY GVFPQPFTDR QYSSYCG