ID   AMYG_SCHPO              Reviewed;         450 AA.
AC   O60087; Q96WS5;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable glucoamylase;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
DE   AltName: Full=Meiotic expression up-regulated protein 17;
DE   Flags: Precursor;
GN   Name=meu17; ORFNames=SPBC14C8.05c;
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 [MRNA] OF 210-450.
RC   STRAIN=CD16-1;
RX   PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA   Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA   Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT   "Comprehensive isolation of meiosis-specific genes identifies novel
RT   proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL   Nucleic Acids Res. 29:2327-2337(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC         successively from non-reducing ends of the chains with release of
CC         beta-D-glucose.; EC=3.2.1.3;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA18423.1; -; Genomic_DNA.
DR   EMBL; AB054301; BAB60870.1; -; mRNA.
DR   PIR; T39433; T39433.
DR   RefSeq; NP_595908.1; NM_001021816.2.
DR   AlphaFoldDB; O60087; -.
DR   SMR; O60087; -.
DR   BioGRID; 276237; 1.
DR   STRING; 4896.SPBC14C8.05c.1; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   PaxDb; O60087; -.
DR   EnsemblFungi; SPBC14C8.05c.1; SPBC14C8.05c.1:pep; SPBC14C8.05c.
DR   GeneID; 2539682; -.
DR   KEGG; spo:SPBC14C8.05c; -.
DR   PomBase; SPBC14C8.05c; meu17.
DR   VEuPathDB; FungiDB:SPBC14C8.05c; -.
DR   eggNOG; ENOG502QPM2; Eukaryota.
DR   HOGENOM; CLU_012173_2_2_1; -.
DR   InParanoid; O60087; -.
DR   OMA; DLTWSYG; -.
DR   PhylomeDB; O60087; -.
DR   PRO; PR:O60087; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0009986; C:cell surface; NAS:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0005628; C:prospore membrane; HDA:PomBase.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; ISO:PomBase.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0005980; P:glycogen catabolic process; ISO:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Meiosis;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001479"
FT   CHAIN           29..450
FT                   /note="Probable glucoamylase"
FT                   /id="PRO_0000001480"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   450 AA;  51164 MW;  31C5BF2A8E4785FE CRC64;
     MRTYWLFLLL GGVVSAESLL SPNKRSKEAS MDEWTDQQKG IAMGHMLNNI GDSGMHAKDI
     NPGCIIASPS TDSPDYYYQW VRDSALTIMT ILDRFFEGDK GLEPIIVKYM DEMVRLQKVP
     NPSGDFYAGG LGEPKFNVDG TSYDGDWGRP QNDSPALRAI AFIKYMNYLF ENGKEVHEVT
     VWIEAVLADL DYTANHWTEA SFDLWEEIKD VHYFTLAVQK RAMQDGTAFA KRIGAPDQAA
     LYQRTIEPID LKLGEFWDPG MGVIKGYKGR VDRSGLDCST LLASLYSNEF DMHILPTLLK
     LQETMTRDYP VNQGWKQAMG RYPEDVYDGV SKSIGNPWFI CTSSAAEIIY KAIAYYDNKG
     LPELTEYNIH FFMKFAEFGD PYNWSVIRKN MHTYADNFLK AVAEFQHPNG SMSEQFSRDD
     GHQKGARDLT WSYSSLLNAI YRREAIKGSV