ID   AMYG_BLAAD              Reviewed;         624 AA.
AC   P42042;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glucoamylase;
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=GAA;
OS   Blastobotrys adeninivorans (Yeast) (Arxula adeninivorans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Blastobotrys.
OX   NCBI_TaxID=409370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LS3;
RA   Bui Minh D., Kunze I., Foerster S., Wartmann T., Horstmann C.,
RA   Manteuffel R., Kunze G.;
RT   "Cloning and expression of an Arxula adeninivorans glucoamylase gene in
RT   Saccharomyces cerevisiae.";
RL   Appl. Microbiol. Biotechnol. 44:610-619(1996).
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; Z46901; CAA86997.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42042; -.
DR   SMR; P42042; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   CLAE; GLA15A_ARXAD; -.
DR   PhylomeDB; P42042; -.
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   Gene3D; 2.60.40.2440; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_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; PS51159; CBM21; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..624
FT                   /note="Glucoamylase"
FT                   /id="PRO_0000001458"
FT   DOMAIN          26..132
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        343
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        582
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   624 AA;  68981 MW;  74C2CDFB43FF71B4 CRC64;
     MRQFLALAAA ASIAVADSCH TFTLANSPPD DKAVALSSYS YCGGYLSASA FVKNLSYDKL
     VTLYWTNADN KSTPLNAGSL DYVKAASDDQ SWELWSLNVT TVPDGVDALL NITYVAASIG
     KTNSQQLNVQ VEATGDPIPT PQIPTIYKPY ASPSDFSDDI TNWLKPSNDS QTGIAKSFLF
     NNINIPGAAP GTVIAAQSYS EPDYAYTWVR DASLVMDVVN RLYSSAKSEE KRQLYEKILF
     QYAKAGAQEQ NDPTAISGMG EPKFYLNNTA FTGSWGRPQN DGPATRAITL IEFANAYLAN
     GGSQDTVREQ LYDSDKYPQV APIKKDLQFV ASNWSSPSFD LWEEEESAHF YTRLVQRKAL
     LLGADFANDM GDHELSDKLK TQASKLSDTL PEFWDSARQL ILYEYGPVLR GKYSYKDISV
     VLGVMHGYAN DNVFSYTNDQ ILATAYQVST SFLDVYKVAN TTSDESGKPL GIPVGRYPED
     VYDGVGTSQG NPWYLTTMAM AEFLYRSVQE FEDAGSIIIS DTSLPFWKYF ASSVDHKAGA
     KYNKNDQSFK TSLKSLTGWG DAFMRRAKYH TPSSGHMSEE FNRTTGEPRG AKDLTWSYAS
     LLSAAFAREE LRNQKNYLTN VADL