ID   AMYG_YEAST              Reviewed;         549 AA.
AC   P08019; D6VVI8; Q07070;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Glucoamylase, intracellular sporulation-specific;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
GN   Name=SGA1; Synonyms=SGA; OrderedLocusNames=YIL099W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3106330; DOI=10.1128/jb.169.5.2142-2149.1987;
RA   Yamashita I., Nakamura M., Fukui S.;
RT   "Gene fusion is a possible mechanism underlying the evolution of STA1.";
RL   J. Bacteriol. 169:2142-2149(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-190.
RC   STRAIN=SPX101-1C;
RX   PubMed=3141213; DOI=10.1016/0014-5793(88)80912-8;
RA   Pardo J.M., Ianez E., Zalacain M., Claros M.G., Jimenez A.;
RT   "Similar short elements in the 5' regions of the STA2 and SGA genes from
RT   Saccharomyces cerevisiae.";
RL   FEBS Lett. 239:179-184(1988).
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; Z38125; CAA86282.1; -; Genomic_DNA.
DR   EMBL; M16166; AAA35042.1; -; Genomic_DNA.
DR   EMBL; X13858; CAA32071.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08454.1; -; Genomic_DNA.
DR   PIR; S48474; S48474.
DR   RefSeq; NP_012167.3; NM_001179447.3.
DR   AlphaFoldDB; P08019; -.
DR   SMR; P08019; -.
DR   BioGRID; 34892; 30.
DR   IntAct; P08019; 1.
DR   MINT; P08019; -.
DR   STRING; 4932.YIL099W; -.
DR   BindingDB; P08019; -.
DR   ChEMBL; CHEMBL1075248; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   PaxDb; 4932-YIL099W; -.
DR   PeptideAtlas; P08019; -.
DR   EnsemblFungi; YIL099W_mRNA; YIL099W; YIL099W.
DR   GeneID; 854708; -.
DR   KEGG; sce:YIL099W; -.
DR   AGR; SGD:S000001361; -.
DR   SGD; S000001361; SGA1.
DR   VEuPathDB; FungiDB:YIL099W; -.
DR   eggNOG; ENOG502QPM2; Eukaryota.
DR   HOGENOM; CLU_012173_2_0_1; -.
DR   InParanoid; P08019; -.
DR   OMA; SHFWNQS; -.
DR   OrthoDB; 1586242at2759; -.
DR   BioCyc; MetaCyc:YIL099W-MONOMER; -.
DR   BioCyc; YEAST:YIL099W-MONOMER; -.
DR   BioGRID-ORCS; 854708; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P08019; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P08019; Protein.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IDA:SGD.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0005980; P:glycogen catabolic process; IMP:SGD.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Sporulation.
FT   CHAIN           1..549
FT                   /note="Glucoamylase, intracellular sporulation-specific"
FT                   /id="PRO_0000186120"
FT   ACT_SITE        261
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        264
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        184
FT                   /note="D -> H (in Ref. 4; CAA32071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504..549
FT                   /note="HVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL -> TW
FT                   EQTGN (in Ref. 1; AAA35042)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  61463 MW;  6351E84F2CF4AB77 CRC64;
     MARQKMFYNK LLGMLSVGFG FAWALENITI YEFDFGKGIL DQSYGGVFSN NGPSQVQLRD
     AVLMNGTVVY DSNGAWDSSA LEEWLQGQKK VSIEKIFENI GPSAVYPSIS PGVVIASPSQ
     THPDYFYQWI RDSALTINSI VSHSAGPAIE TLLQYLNVSF HLQRSNNTLG AGIGYTNDTV
     ALGDPKWNVD NTAFTEDWGR PQNDGPALRS IAILKIIDYI KQSGTDLGAK YPFQSTADIF
     DDIVRWDLRF IIDHWNSSGF DLWEEVNGMH FFTLLVQLSA VDKSLSYFNA SERSSPFVEE
     LRQTRRDISK FLVDPANGFI NGKYNYIVGT PMIADTLRSG LDISTLLAAN TVHDAPSASH
     LPFDINDPAV LNTLHHLMLH MRSIYPINDS SKNATGIALG RYPEDVYDGY GFGEGNPWVL
     ATCTASTTLY QLIYRHISEQ HDLVVPMNND CSNAFWSELV FSNLTTLGND EGYLILEFNT
     PAFNQTIQKI FQLADSFLVK LKAHVGTDGE LSEQFNKYTG FMQGAQHLTW SYTSFWDAYQ
     IRQEVLQSL
//