ID   AMYH_SACFI              Reviewed;         519 AA.
AC   P26989; P78745;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Glucoamylase GLA1;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
DE   Flags: Precursor;
GN   Name=GLA1;
OS   Saccharomycopsis fibuligera (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycopsidaceae; Saccharomycopsis.
OX   NCBI_TaxID=4944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KZ;
RX   PubMed=1840532; DOI=10.1016/0378-1097(91)90452-g;
RA   Hostinova E., Balanova J., Gasperik J.;
RT   "The nucleotide sequence of the glucoamylase gene GLA1 from
RT   Saccharomycopsis fibuligera KZ.";
RL   FEMS Microbiol. Lett. 67:103-108(1991).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=KZ;
RA   Hostinova E.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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; X58117; CAA41120.1; -; Genomic_DNA.
DR   AlphaFoldDB; P26989; -.
DR   SMR; P26989; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
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..27
FT   CHAIN           28..519
FT                   /note="Glucoamylase GLA1"
FT                   /id="PRO_0000001476"
FT   ACT_SITE        234
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   519 AA;  57542 MW;  A15A009A7640053C CRC64;
     MRFGVLISVF VAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD KQKDVSLYYL
     LQNIAYPEGQ FNDGVPGTVI ASPSTSNPDY YYQWTRDSAI TFLTVLSELE DNNFNTTLAK
     AVEYYINTSY NLQRTSNPSG SFDDENHKGL GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA
     ISRYLNDVNS LNKGKLVLTD SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ
     GRHFFTSLVQ QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV
     ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL LEDNKDRYSV
     NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP YKLVYDAKSA SNDITINKIN
     YDFFNKYIVD LSTINSGYQS SDSVTIKSGS DEFNTVADNL VTFGDSFLQV ILDHINDDGS
     LNEQLNRNTG YSTSAYSLTW SSGALLEAIR LRNKVKALA