ID   AGLU_ASPOR              Reviewed;         985 AA.
AC   Q12558; Q7LWA9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Alpha-glucosidase;
DE            Short=AGL;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
GN   Name=agdA; ORFNames=AO090003001209;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=7549103; DOI=10.1271/bbb.59.1516;
RA   Minetoki T., Gomi K., Kitamoto K., Kumagai C., Tamura G.;
RT   "Nucleotide sequence and expression of alpha-glucosidase-encoding gene
RT   (agdA) from Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 59:1516-1521(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=10830498; DOI=10.1271/bbb.64.816;
RA   Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N.,
RA   Iimura Y.;
RT   "Molecular cloning and characterization of a transcriptional activator
RT   gene, amyR, involved in the amylolytic gene expression in Aspergillus
RT   oryzae.";
RL   Biosci. Biotechnol. Biochem. 64:816-827(2000).
RN   [3]
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   -!- FUNCTION: Hydrolyzes malto-oligosaccharides, but has a low activity
CC       toward soluble starch.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- INDUCTION: By maltose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; D45179; BAA08125.1; -; Genomic_DNA.
DR   EMBL; AB021876; BAA95702.1; -; Genomic_DNA.
DR   EMBL; AP007155; BAE58289.1; -; Genomic_DNA.
DR   PIR; JC4217; JC4217.
DR   RefSeq; XP_001820291.1; XM_001820239.2.
DR   AlphaFoldDB; Q12558; -.
DR   SMR; Q12558; -.
DR   STRING; 510516.Q12558; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GlyCosmos; Q12558; 16 sites, No reported glycans.
DR   EnsemblFungi; BAE58289; BAE58289; AO090003001209.
DR   GeneID; 5992274; -.
DR   KEGG; aor:AO090003001209; -.
DR   VEuPathDB; FungiDB:AO090003001209; -.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   OMA; PYVINHD; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IMP:AspGD.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046527; F:glucosyltransferase activity; IDA:AspGD.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IC:AspGD.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..985
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000018577"
FT   ACT_SITE        492
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        660
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        661
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        835
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        881
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        929
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        957
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   985 AA;  108704 MW;  3E9EAE0A0E38209E CRC64;
     MAGLKSFLAS SWLLPVACGA SQSIVPSTSA TAAYSQFTIP ASADVGANLV ANIDDPQAVN
     AQSVCPGYKA SDVKHSSQGF TASLELAGDP CNVYGTDVDS LTLTVEYQAK DRLNIQIVPT
     YFDASNASWY ILSEELVPRP KASQNASVPQ SDFVVSWSNE PSFNFKVIRK ATGDVLFNTK
     GSTLVYENQF IEFVTLLPEE YNLYGLGERM NQLRLLENAN LTLYAADIAD PIDDNIYGHH
     AFYLDTRYYK VGGQNKSHTI VKSSEAEPSQ EYVSYSHGVF LRNAHGQEIL LRDQKLIWRT
     LGGSVDLTFY SGPTQAEVTK QYQLSTVGLP AMQQYNTLGF HQCRWGYNNW SEFEDVLANF
     ERFEIPLEYL WADIDYMHGY RNFDNDQHRF SYEEGEKFLN KLHAGGRRWV PIVDGALYIP
     NPENASDAYE TYDRGAKDDV FIKNPDGSLY IGAVWPGYTV YPDWHHPKAS DFWANELVTW
     WNKLHYDGVW YDMAEVSSFC VGSCGTGNLS MNPAHPPFAL PGEPGNVVYD YPEGFNITNA
     TEAASASAGA ASQSAAASST TTSAPYLRTT PTPGVRNVDH PPYVINHVQP GHDLSVHAIS
     PNSTHSDGVQ EYDVHSLYGH QGINATYHGL LKVWENKRPF IIARSTFSGS GKWAGHWGGD
     NFSKWGSMFF SISQALQFSL FGIPMFGVDT CGFNGNTDEE LCNRWMQLSA FFPFYRNHNV
     LSAIPQEPYR WASVIDATKA AMNIRYAILP YFYTLFHLAH TTGSTVMRAL AWEFPNDPSL
     AAVGTQFLVG PSVMVIPVLE PQVDTVQGVF PGVGHGEVWY DWYSQTAVDA KPGVNTTISA
     PLGHIPVFVR GGSILPMQEV ALTTRDARKT PWSLLASLSS NGTASGQLYL DDGESVYPED
     TLSVDFLASR STLRASARGT WKEANPLANV TVLGVTEKPS SVTLNGETLS SDSVKYNATS
     HVLHVGGLQK HTADGAWAKD WVLKW
//