EXG2_SCHPO
ID EXG2_SCHPO Reviewed; 570 AA.
AC Q10444;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Glucan 1,3-beta-glucosidase 2;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase 2;
DE Flags: Precursor;
GN Name=exg2; ORFNames=SPAC12B10.11;
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).
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; CU329670; CAA94701.1; -; Genomic_DNA.
DR PIR; T37578; T37578.
DR RefSeq; NP_594643.1; NM_001020071.1.
DR AlphaFoldDB; Q10444; -.
DR SMR; Q10444; -.
DR BioGRID; 279425; 2.
DR STRING; 4896.SPAC12B10.11.1; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; Q10444; -.
DR EnsemblFungi; SPAC12B10.11.1; SPAC12B10.11.1:pep; SPAC12B10.11.
DR GeneID; 2542987; -.
DR KEGG; spo:SPAC12B10.11; -.
DR PomBase; SPAC12B10.11; exg2.
DR VEuPathDB; FungiDB:SPAC12B10.11; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_2_1; -.
DR InParanoid; Q10444; -.
DR OMA; THQYTIF; -.
DR PhylomeDB; Q10444; -.
DR PRO; PR:Q10444; -.
DR Proteomes; UP000002485; Chromosome I.
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; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IGI:PomBase.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:PomBase.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000007895"
FT CHAIN 48..570
FT /note="Glucan 1,3-beta-glucosidase 2"
FT /id="PRO_0000007896"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 570 AA; 65687 MW; 2B6E66A35AA7E1E8 CRC64;
MSNLLEAESS CDSKSLGVDD FTSKRCREID KKALLITILL TFFVSLCVFL SIILPLIFLV
IIPHAQSDRK IKDTNMETTN LGVNIIDEIF NSTQVPEWAK NSLLDTNTWL DTSDFNTSFT
NETFAGLYTM GIFDKYDDSV QANPNVPPLN EPFPYGRLPI RGVNLGGWLS MEPFITPSFF
QVKNETAYLV KDELSLHAYL GENATSVIEN HYNTFVTKQT FYEIREAGLD HVRITFPYWI
LYSNEITNVS GIGWRYLLRS IEWAREQGLR VNLDLHAAPG NQNSWNHGGY LNQMEWLDGT
VKGEENSQFT LKIHERLASF FSQKRYRNVV TIYGALNEPN FFVLDEHKIT DWHKQAYAVI
RQSNFTGLIS LSDGFRGPGN WEDHFDPFHF PNILIDVHRY IIFNDFLIGL RPKDKLNVIC
KSWNEEMKLK AKLPTIIGEW SLADTDCAKF LNNVGEGARW DGTFTPNGGV ASCSEKVGCR
CDFANQDPEN YEDSYRKFLY ALATSQIETF DKTWGWFYWN WDTENATQWS YKKSWLAGLL
PRLAYSTTKD FNCSMLDSKS FMEFDEQSEF
