ID   AMYH_YEASX              Reviewed;         767 AA.
AC   P04065; Q92314;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   22-FEB-2023, entry version 109.
DE   RecName: Full=Glucoamylase S1;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=GAI;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
DE   Flags: Precursor;
GN   Name=STA1; Synonyms=DEX2, MAL5;
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 / ATCC 60709 / 5106-9A;
RX   PubMed=3918017; DOI=10.1128/jb.161.2.567-573.1985;
RA   Yamashita I., Suzuki K., Fukui S.;
RT   "Nucleotide sequence of the extracellular glucoamylase gene STA1 in the
RT   yeast Saccharomyces diastaticus.";
RL   J. Bacteriol. 161:567-573(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX   AGRICOLA=IND86044727;
RA   Yamashita I., Suzuki K., Sakuzo F.;
RT   "Proteolytic processing of glucoamylase in the yeast Saccharomyces
RT   cerevisiae.";
RL   Agric. Biol. Chem. 50:475-482(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RA   Shima H., Inui M., Akada R., Yamashita I.;
RT   "Upstream regions of the yeast glucoamylase gene which are required for
RT   efficient transcription.";
RL   Agric. Biol. Chem. 53:749-755(1989).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X02649; CAA26487.1; ALT_INIT; Genomic_DNA.
DR   EMBL; D00428; BAA00332.1; -; Genomic_DNA.
DR   PIR; A21896; ALBYG.
DR   AlphaFoldDB; P04065; -.
DR   SMR; P04065; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   GlyCosmos; P04065; 12 sites, No reported glycans.
DR   VEuPathDB; FungiDB:YIL099W; -.
DR   BRENDA; 3.2.1.3; 5495.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IMP:SGD.
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..767
FT                   /note="Glucoamylase S1"
FT                   /id="PRO_0000001477"
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          348..691
FT                   /note="H subunit"
FT   REGION          692..767
FT                   /note="Y subunit"
FT   ACT_SITE        518
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        521
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         455
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        645
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        650
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        741
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   767 AA;  82489 MW;  A5F29E2427EDB593 CRC64;
     MQRPFLLAYL VLSLLFNSAL GFPTALVPRG SSSSNITSSG PSSTPFSSAT ESFSTGTTVT
     PSSSKYPGSK TETSVSSTTE TTIVPTTTTT SVITPSTTTI TTTVCSTGTN SAGETTSGCS
     PKTITTTVPC STSPSETASE STTTSPTTPV TTVVSTTVVT TEYSTSTKQG GEITTTFVTK
     NIPTTYLTTI APTSSVTTVT NFTPTTITTT VCSTGTNSAG ETTSGCSPKT VTTTVPCSTG
     TGEYTTEATA PVTTAVTTTV VTTESSTGTN SAGKTTTSYT TKSVPTTYVF DFGKGILDQS
     CGGVFSNNGS SQVQLRDVVL MNGTVVYDSN GAWDSSALEE WLQRQKKVSI ERIFENIGPS
     AVYPSILPGV VIASPSQTHP DYFYQWIRDS ALTINSIVSH SADPAIETLL QYLNVSFHLQ
     RTNNTLGAGI GYTNDTVALG DPKWNVDNTA FTEPWGRPQN DGPALRSIAI LKIIDYIKQS
     GTDLGAKYPF QSTADIFDDI VRWDLRFIID HWNSSGFDLW EEVNGMHFFT LLVQLSAVDR
     SLSYFNASER SSPFVEELRQ TRRDISKFLV DPANGFINGK YNYIVETPMI ADTLRSGLDI
     STLLAANTVH DAPSASHLPF DINDPAVLNT LHHLMLHMRS IYPINDSSKN ATGIALGRYP
     EDVYDGYGVG EGNPWVLATC AASTTLYQLI YRHISEQHDL VVPMNNDCSN AFWSELVFSN
     LTTLGNDEGY LILEFNTPAF NQTIQKIFQL ADSFLVKLKA TWEQTGN
//