AMYI_YEASX
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 03-AUG-2022, entry version 95.
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 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 Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; SSF48208; 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
