AMYG_ASPNG
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 03-AUG-2022, entry version 100.
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 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 STRING; 5061.CADANGAP00003574; -.
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 VEuPathDB; FungiDB:An03g06550; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1166799; -.
DR VEuPathDB; FungiDB:ATCC64974_75950; -.
DR VEuPathDB; FungiDB:M747DRAFT_339326; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
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; -; 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; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
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; SSF48208; 1.
DR SUPFAM; SSF49452; SSF49452; 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
