BGL2_SCHPO
ID BGL2_SCHPO Reviewed; 321 AA.
AC O13990; P79062;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 4.
DT 03-AUG-2022, entry version 122.
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=bgl2; ORFNames=SPAC26H5.08c;
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 11-321.
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: Glucanases possibly play a role in cell expansion during
CC growth, in cell-cell fusion during mating, and in spore release during
CC sporulation. This enzyme may be involved in beta-glucan degradation and
CC also function biosynthetically as a transglycosylase.
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, cell wall {ECO:0000250}. Note=Tightly
CC bound to cell wall. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB16200.1; -; Genomic_DNA.
DR EMBL; AB000539; BAA19145.1; ALT_INIT; mRNA.
DR PIR; T38427; T38427.
DR RefSeq; NP_594455.1; NM_001019884.2.
DR AlphaFoldDB; O13990; -.
DR SMR; O13990; -.
DR BioGRID; 279153; 20.
DR STRING; 4896.SPAC26H5.08c.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR MaxQB; O13990; -.
DR PaxDb; O13990; -.
DR EnsemblFungi; SPAC26H5.08c.1; SPAC26H5.08c.1:pep; SPAC26H5.08c.
DR GeneID; 2542700; -.
DR KEGG; spo:SPAC26H5.08c; -.
DR PomBase; SPAC26H5.08c; bgl2.
DR VEuPathDB; FungiDB:SPAC26H5.08c; -.
DR eggNOG; ENOG502QQE6; Eukaryota.
DR HOGENOM; CLU_028820_2_1_1; -.
DR InParanoid; O13990; -.
DR OMA; WKPDTSG; -.
DR PhylomeDB; O13990; -.
DR PRO; PR:O13990; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; ISO:PomBase.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; ISO:PomBase.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IC:PomBase.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..321
FT /note="Glucan 1,3-beta-glucosidase"
FT /id="PRO_0000011895"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 281
FT /note="D -> N (in Ref. 2; BAA19145)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> L (in Ref. 2; BAA19145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35412 MW; 10094466592006CA CRC64;
MQFLSSFVFA ALALLPLSAM AVDEAASEIA SSTKPASTNG TLSFCLGVKH ADGTCKYTDD
YLADFEVLAP YTNMIRTYAT SDCNTLEYLL PALAQSPYNF SAILGVWPTD DAHYDLEKQA
LMQYLPQYGV DHVRAITVGS EVLYRNDLPA DVLAERIYDV RGLVQQKLGF DVPVGTADSW
NLWAGGSGDV VITASDFIMS NDFPYWQGQN TSNMTNTFIS DTLAALERVQ SVKGTNNVTF
WVGETGWPTD GPSYGEADAT VDIASEFFQE ALCNIRRKGI DIFFFEAFDE DWKGDSSSVE
PYFGAMYSNR TLKYNLNCTS E
