AGLU_ASPOR
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 25-MAY-2022, entry version 107.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 EnsemblFungi; BAE58289; BAE58289; AO090003001209.
DR GeneID; 5992274; -.
DR KEGG; aor:AO090003001209; -.
DR VEuPathDB; FungiDB:AO090003001209; -.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; YDTYTRG; -.
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:0044264; P:cellular polysaccharide metabolic process; IC:AspGD.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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
