AMYH_YEASX
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 03-AUG-2022, entry version 107.
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 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 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..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
