ID   AMYG_ASPKA              Reviewed;         639 AA.
AC   P23176;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Glucoamylase I;
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=gaI;
OS   Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1069201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   DOI=10.1271/bbb1961.53.923;
RA   Hayashida S., Kuroda K., Ohta K., Kuhara S., Fukuda K., Sakaki Y.;
RT   "Molecular cloning of the glucoamylase I gene of Aspergillus awamori var.
RT   kawachi for localization of the raw-starch-affinity site.";
RL   Agric. Biol. Chem. 53:923-929(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 494-538.
RX   DOI=10.1271/bbb1961.53.135;
RA   Hayashida S., Nakahara K., Kuroda K., Miyata T., Iwanaga S.;
RT   "Structure of the raw-starch-affinity site on the Aspergillus awamori var.
RT   kawachi glucoamylase I molecule.";
RL   Agric. Biol. Chem. 53:135-141(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}.
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DR   EMBL; D00427; BAA00331.1; -; Genomic_DNA.
DR   PIR; JT0479; JT0479.
DR   AlphaFoldDB; P23176; -.
DR   BMRB; P23176; -.
DR   SMR; P23176; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   GlyConnect; 173; 4 O-Linked glycans.
DR   GlyCosmos; P23176; 39 sites, 9 glycans.
DR   VEuPathDB; FungiDB:AKAW_08979; -.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT   PROPEP          19..24
FT                   /id="PRO_0000001463"
FT   CHAIN           25..639
FT                   /note="Glucoamylase I"
FT                   /id="PRO_0000001464"
FT   DOMAIN          532..639
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   REGION          494..531
FT                   /note="Raw-starch-adsorbable GP-I sequence"
FT   REGION          497..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        464
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        466
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        467
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        475
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        476
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        482
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        483
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        485
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        487
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        491
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        495
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        498
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        499
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        500
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        501
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        503
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        505
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        507
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        511
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        512
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        513
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        514
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        516
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        517
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        519
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        521
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        523
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        524
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        525
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        526
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        527
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        528
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        529
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        530
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        531
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        533
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        534
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        233..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        245..472
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..293
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   639 AA;  68272 MW;  E112B31A4DD8DD6B CRC64;
     MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI
     VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS TIEHYISSQA IIQGVSNPSG
     DLSSGGLGEP KFNVDETAYT GSWGRPQRDG PALRATAMIG FGQVLLDNGY TSAATEIVWP
     LVRNDLSYVA QYWNQTGYDL WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA
     PQILCYLQSF WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
     HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ LYDALYQWDK
     QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV KTFADGFVSI VETHAASNGS
     LSEQFDKSDG DELSARDLTW SYAALLTANN RRNSVVPPSW GETSASSWPG TCAATSASGT
     YSSVTVTSWP SIVATGGTTT TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV
     TFDLTATTTY GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY
     KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR
//