AMYG_ASPOR
ID AMYG_ASPOR Reviewed; 612 AA.
AC P36914; Q3HLW7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
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; Synonyms=gluB; ORFNames=AO090010000746;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1368680; DOI=10.1271/bbb1961.55.941;
RA Hata Y., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S.;
RT "The glucoamylase cDNA from Aspergillus oryzae: its cloning, nucleotide
RT sequence, and expression in Saccharomyces cerevisiae.";
RL Agric. Biol. Chem. 55:941-949(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=1761224; DOI=10.1016/0378-1119(91)90500-b;
RA Hata Y., Tsuchiya K., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S.;
RT "Nucleotide sequence and expression of the glucoamylase-encoding gene
RT (glaA) from Aspergillus oryzae.";
RL Gene 108:145-150(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ma L., Chen D., Chen X., Wang H.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; D01035; BAA00841.1; -; mRNA.
DR EMBL; D10698; BAA01540.1; -; Genomic_DNA.
DR EMBL; DQ211971; ABA62323.1; -; mRNA.
DR EMBL; AP007175; BAE66563.1; -; Genomic_DNA.
DR PIR; JQ1346; JQ1346.
DR RefSeq; XP_001827696.1; XM_001827644.2.
DR AlphaFoldDB; P36914; -.
DR SMR; P36914; -.
DR STRING; 510516.P36914; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR EnsemblFungi; BAE66563; BAE66563; AO090010000746.
DR GeneID; 5999830; -.
DR KEGG; aor:AO090010000746; -.
DR VEuPathDB; FungiDB:AO090010000746; -.
DR HOGENOM; CLU_012173_1_0_1; -.
DR OMA; HAANAKP; -.
DR BRENDA; 3.2.1.3; 522.
DR Proteomes; UP000006564; Chromosome 8.
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 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT PROPEP 20..25
FT /evidence="ECO:0000250"
FT /id="PRO_0000001465"
FT CHAIN 26..612
FT /note="Glucoamylase"
FT /id="PRO_0000001466"
FT DOMAIN 506..612
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 236..239
FT /evidence="ECO:0000250"
FT DISULFID 248..475
FT /evidence="ECO:0000250"
FT DISULFID 288..296
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="G -> S (in Ref. 1; BAA00841 and 2; BAA01540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 65457 MW; 7C36E1B0A341CEDA CRC64;
MVSFSSCLRA LALGSSVLAV QPVLRQATGL DTWLSTEANF SRQAILNNIG ADGQSAQGAS
PGVVIASPSK SDPDYFYTWT RDSGLVMKTL VDLFRGGDAD LLPIIEEFIS SQARIQGISN
PSGALSSGGL GEPKFNVDET AFTGAWGRPQ RDGPALRATA MISFGEWLVE NGHTSIATDL
VWPVVRNDLS YVAQYWSQSG FDLWEEVQGT SFFTVAVSHR ALVEGSSFAK TVGSSCPYCD
SQAPQVRCYL QSFWTGSYIQ ANFGGGRSGK DINTVLGSIH TFDPQATCDD ATFQPCSARA
LANHKVVTDS FRSIYAINSG RAENQAVAVG RYPEDSYYNG NPWFLTTLAA AEQLYDALYQ
WDKIGSLAIT DVSLPFFKAL YSSAATGTYA SSTTVYKDIV SAVKAYADGY VQIVQTYAAS
TGSMAEQYTK TDGSQTSARD LTWSYAALLT ANNRRNAVVP APWGETAATS IPSACSTTSA
SGTYSSVVIT SWPTISGYPG APDSPCQVPT TVSVTFAVKA TTVYGESIKI VGSISQLGSW
NPSSATALNA DSYTTDNPLW TGTINLPAGQ SFEYKFIRVQ NGAVTWESDP NRKYTVPSTC
GVKSAVQSDV WR
