ID   AMYG_ASPNG              Reviewed;         640 AA.
AC   P69328; P04064; Q92201; Q99179;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=GLAA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2).
RX   PubMed=6204865; DOI=10.1002/j.1460-2075.1984.tb02014.x;
RA   Boel E., Hansen M.T., Hjort I., Hoegh I., Fiil N.P.;
RT   "Two different types of intervening sequences in the glucoamylase gene from
RT   Aspergillus niger.";
RL   EMBO J. 3:1581-1585(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2).
RX   PubMed=6203744; DOI=10.1002/j.1460-2075.1984.tb01935.x;
RA   Boel E., Hjort I., Svensson B., Norris F., Norris K.E., Fiil N.P.;
RT   "Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two
RT   different but closely related mRNAs.";
RL   EMBO J. 3:1097-1102(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-640, AND COMPARISON OF FORMS G1 AND G2.
RX   PubMed=3081341; DOI=10.1111/j.1432-1033.1986.tb09425.x;
RA   Svensson B., Larsen K., Gunnarsson A.;
RT   "Characterization of a glucoamylase G2 from Aspergillus niger.";
RL   Eur. J. Biochem. 154:497-502(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-640 (ISOFORM G1), AND GLYCOSYLATION.
RA   Svensson B., Larsen K., Svendsen I., Boel E.;
RT   "The complete amino acid sequence of the glycoprotein, glucoamylase G1,
RT   from Aspergillus niger.";
RL   Carlsberg Res. Commun. 48:529-544(1983).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-11.
RC   STRAIN=ATCC 10864 / NRRL 330 / CBS 122.49 / NBRC 6661 / NRRL 330;
RX   PubMed=2076554; DOI=10.1007/bf00327025;
RA   Fowler T., Berka R.M., Ward M.;
RT   "Regulation of the glaA gene of Aspergillus niger.";
RL   Curr. Genet. 18:537-545(1990).
RN   [6]
RP   CONFORMATION OF O-GLYCOSYLATED REGION.
RX   PubMed=1546955; DOI=10.1042/bj2820423;
RA   Williamson G., Belshaw N.J., Williamson M.P.;
RT   "O-glycosylation in Aspergillus glucoamylase. Conformation and role in
RT   binding.";
RL   Biochem. J. 282:423-428(1992).
RN   [7]
RP   CHARACTERIZATION OF CATALYTIC DOMAIN.
RX   PubMed=8503847; DOI=10.1042/bj2920197;
RA   Stoffer B., Frandsen T.P., Busk P.K., Schneider P., Svendsen I.,
RA   Svensson B.;
RT   "Production, purification and characterization of the catalytic domain of
RT   glucoamylase from Aspergillus niger.";
RL   Biochem. J. 292:197-202(1993).
RN   [8]
RP   STRUCTURE BY NMR OF 533-640.
RX   PubMed=8683599; DOI=10.1006/jmbi.1996.0374;
RA   Sorimachi K., Jacks A.J., le Gal-Coeffet M.-F., Williamson G., Archer D.B.,
RA   Williamson M.P.;
RT   "Solution structure of the granular starch binding domain of glucoamylase
RT   from Aspergillus niger by nuclear magnetic resonance spectroscopy.";
RL   J. Mol. Biol. 259:970-987(1996).
RN   [9]
RP   STRUCTURE BY NMR OF 533-640.
RX   PubMed=9195884; DOI=10.1016/s0969-2126(97)00220-7;
RA   Sorimachi K., le Gal-Coeffet M.-F., Williamson G., Archer D.B.,
RA   Williamson M.P.;
RT   "Solution structure of the granular starch binding domain of Aspergillus
RT   niger glucoamylase bound to beta-cyclodextrin.";
RL   Structure 5:647-661(1997).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=G1;
CC         IsoId=P69328-1; Sequence=Displayed;
CC       Name=G2;
CC         IsoId=P69328-2; Sequence=VSP_012837, VSP_012838;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; X00548; CAA25219.1; -; mRNA.
DR   EMBL; X00712; CAA25303.1; -; Genomic_DNA.
DR   EMBL; X00712; CAA25304.1; -; Genomic_DNA.
DR   EMBL; X56442; CAA39825.1; -; Genomic_DNA.
DR   PIR; A90986; ALASGR.
DR   RefSeq; XP_001390530.1; XM_001390493.2. [P69328-1]
DR   PDB; 1AC0; NMR; -; A=533-640.
DR   PDB; 1ACZ; NMR; -; A=533-640.
DR   PDB; 1KUL; NMR; -; A=533-640.
DR   PDB; 1KUM; NMR; -; A=533-640.
DR   PDB; 3EQA; X-ray; 1.90 A; A=25-494.
DR   PDB; 5GHL; X-ray; 2.00 A; A/B/C/D=533-640.
DR   PDB; 6FRV; X-ray; 2.30 A; A=25-640.
DR   PDBsum; 1AC0; -.
DR   PDBsum; 1ACZ; -.
DR   PDBsum; 1KUL; -.
DR   PDBsum; 1KUM; -.
DR   PDBsum; 3EQA; -.
DR   PDBsum; 5GHL; -.
DR   PDBsum; 6FRV; -.
DR   AlphaFoldDB; P69328; -.
DR   BMRB; P69328; -.
DR   SMR; P69328; -.
DR   BindingDB; P69328; -.
DR   ChEMBL; CHEMBL3745; -.
DR   Allergome; 914; Asp n Glucoamylase.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   CLAE; GLA15A_ASPNG; -.
DR   GlyConnect; 175; 4 O-Linked glycans.
DR   GlyCosmos; P69328; 41 sites, 7 glycans.
DR   PaxDb; 5061-CADANGAP00003574; -.
DR   EnsemblFungi; CAK38411; CAK38411; An03g06550. [P69328-1]
DR   GeneID; 4980642; -.
DR   VEuPathDB; FungiDB:An03g06550; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1166799; -.
DR   VEuPathDB; FungiDB:ATCC64974_75950; -.
DR   VEuPathDB; FungiDB:M747DRAFT_339326; -.
DR   eggNOG; ENOG502QPM2; Eukaryota.
DR   OrthoDB; 1586242at2759; -.
DR   BRENDA; 3.2.1.3; 518.
DR   EvolutionaryTrace; P69328; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:AspGD.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IMP:AspGD.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IMP:AspGD.
DR   CDD; cd05811; CBM20_glucoamylase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034836; CBM20_glucoamylase.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   InterPro; IPR046966; Glucoamylase_active_site.
DR   InterPro; IPR008291; Glucoamylase_SBD.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1.
DR   PANTHER; PTHR31616; TREHALASE; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PIRSF; PIRSF001031; Glu-a-glcsd_SBD; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000269|PubMed:3081341"
FT                   /id="PRO_0000001461"
FT   CHAIN           25..640
FT                   /note="Glucoamylase"
FT                   /id="PRO_0000001462"
FT   DOMAIN          533..640
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   REGION          498..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        465
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        467
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        468
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        476
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        477
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        483
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        484
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        486
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        488
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        489
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        492
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        496
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        499
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        500
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        501
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        502
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        504
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        506
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        508
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        510
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        512
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        513
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        514
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        515
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        517
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        518
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        520
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        522
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        524
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        525
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        526
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        527
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        528
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        529
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        530
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        531
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        532
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        534
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CARBOHYD        535
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   DISULFID        234..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        246..473
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..294
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         527..534
FT                   /note="STSSTSCT -> TTRSGMSL (in isoform G2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012837"
FT   VAR_SEQ         535..640
FT                   /note="Missing (in isoform G2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012838"
FT   HELIX           31..44
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           77..92
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           150..168
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           172..177
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           179..193
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           210..229
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           235..248
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          254..257
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:6FRV"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           296..307
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            308..312
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           342..362
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          364..367
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            369..371
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           372..378
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          384..388
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           392..415
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   TURN            428..430
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          433..438
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           440..453
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   HELIX           463..465
FT                   /evidence="ECO:0007829|PDB:3EQA"
FT   STRAND          537..546
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          554..561
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   HELIX           562..564
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   TURN            565..567
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   HELIX           569..571
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          572..574
FT                   /evidence="ECO:0007829|PDB:1KUL"
FT   STRAND          578..583
FT                   /evidence="ECO:0007829|PDB:1AC0"
FT   STRAND          586..594
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          595..597
FT                   /evidence="ECO:0007829|PDB:1AC0"
FT   STRAND          598..606
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          608..610
FT                   /evidence="ECO:0007829|PDB:1AC0"
FT   STRAND          612..614
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          620..623
FT                   /evidence="ECO:0007829|PDB:5GHL"
FT   STRAND          626..629
FT                   /evidence="ECO:0007829|PDB:1AC0"
FT   STRAND          632..638
FT                   /evidence="ECO:0007829|PDB:5GHL"
SQ   SEQUENCE   640 AA;  68309 MW;  26F58DD18AD7F702 CRC64;
     MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI
     VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS TIENYISAQA IVQGISNPSG
     DLSSGAGLGE PKFNVDETAY TGSWGRPQRD GPALRATAMI GFGQWLLDNG YTSTATDIVW
     PLVRNDLSYV AQYWNQTGYD LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ
     APEILCYLQS FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA
     NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE QLYDALYQWD
     KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA VKTFADGFVS IVETHAASNG
     SMSEQYDKSD GEQLSARDLT WSYAALLTAN NRRNSVVPAS WGETSASSVP GTCAATSAIG
     TYSSVTVTSW PSIVATGGTT TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA
     VTFDLTATTT YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE
     YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR
//