ID   AMYI_YEASX              Reviewed;         768 AA.
AC   P29760;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   22-FEB-2023, entry version 97.
DE   RecName: Full=Glucoamylase S2;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=GAII;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
DE   Flags: Precursor;
GN   Name=STA2; Synonyms=DEX1;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Diastaticus;
RX   PubMed=8017901; DOI=10.1007/bf02921653;
RA   Kim K., Bajszar G., Lee S.Y., Knudsen F., Mattoon J.R.;
RT   "Cloning of a new allelic variant of a Saccharomyces diastaticus
RT   glucoamylase gene and its introduction into industrial yeasts.";
RL   Appl. Biochem. Biotechnol. 44:161-185(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Diastaticus;
RX   PubMed=2055484; DOI=10.1016/0378-1119(91)90354-e;
RA   Lambrechts M.G., Pretorius I.S., Sollitti P., Marmur J.;
RT   "Primary structure and regulation of a glucoamylase-encoding gene (STA2) in
RT   Saccharomyces diastaticus.";
RL   Gene 100:95-103(1991).
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; M60650; AAA35107.1; -; Genomic_DNA.
DR   EMBL; M90490; AAA20560.1; -; Genomic_DNA.
DR   PIR; JU0474; JU0474.
DR   AlphaFoldDB; P29760; -.
DR   SMR; P29760; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   GlyCosmos; P29760; 12 sites, No reported glycans.
DR   VEuPathDB; FungiDB:YIL099W; -.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; 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   InterPro; IPR046966; Glucoamylase_active_site.
DR   PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 1.
DR   PANTHER; PTHR31616; TREHALASE; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..768
FT                   /note="Glucoamylase S2"
FT                   /id="PRO_0000001478"
FT   REGION          29..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..692
FT                   /note="H subunit"
FT   REGION          693..768
FT                   /note="Y subunit"
FT   ACT_SITE        519
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        522
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        35
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        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        651
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        742
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        164
FT                   /note="Missing (in Ref. 1; AAA35107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="D -> N (in Ref. 1; AAA35107)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   768 AA;  82587 MW;  3FAC172C128A0C6F CRC64;
     MQRPFLLAYL VLSLLFNSAL GFPTALVPRG SSSSNITSSG PSSTPFSSAT ESFSTGTTVT
     PSSSKYPGSK TETSVSSTTE TTIVPTTTTT SVITPSTTTI TTTVCSTGTN SAGETTSGCS
     PKTITTTVPC STSPSETASE STTTSPTTPV TTVVSTTVVT TEYASTSTKQ GGEITTTFVT
     KNIPTTYLTT IAPTSSVTTV TNFTPTTITT TVCSTGTNSA GETTSGCSPK TVTTTVPCST
     GTGEYTTEAT APVTTAVTTT VVTTESSTGT NSAGKTTTSY TTKSVPTTYV FDFGKGILDQ
     SCGGVFSNNG SSQVQLRDVV LMNGTVVYDS NGAWDSSPLE EWLQRQKKVS IERIFENIGP
     SAVYPSILPG VVIASPSQTH PDYFYQWIRD SALTINSIVS HSADPAIETL LQYLNVSFHL
     QRTNNTLGAG IGYTNDTVAL GDPKWNVDNT AFTEPWGRPQ NDGPALRSIA ILKIIDYIKQ
     SGTDLGAKYP FQSTADIFDD IVRWDLRFII DHWNSSGFDL WEEVNGMHFF TLLVQLSAVD
     RSLSYFNASE RSSPFVEELR QTRRDISKFL VDPANGFING KYNYIVETPM IADTLRSGLD
     ISTLLAANTV HDAPSASHLP FDIDDPAVLN TLHHLMLHMR SIYPINDSSK NATGIALGRY
     PEDVYDGYGV GEGNPWVLAT CAASTTLYQL IYRHISEQHD LVVPMNNDCS NAFWSELVFS
     NLTTLGNDEG YLILEFNTPA FNQTIQKIFQ LADSFLVKLK ATWEQTGN
//