ID   AGL_PEDPE               Reviewed;         557 AA.
AC   P43473;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Alpha-glucosidase;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
GN   Name=agl;
OS   Pediococcus pentosaceus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=1255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPE1.0;
RA   Leenhouts K.K.J., Bolhuis A.A., Kok J.J., Venema G.G.;
RT   "The sucrose and raffinose operons of Pediococcus pentosaceus PPE1.0.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 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; Z32771; CAA83671.1; -; Genomic_DNA.
DR   EMBL; L32093; AAA25570.1; -; Genomic_DNA.
DR   PIR; S77969; S77969.
DR   AlphaFoldDB; P43473; -.
DR   SMR; P43473; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..557
FT                   /note="Alpha-glucosidase"
FT                   /id="PRO_0000054335"
FT   ACT_SITE        201
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            332
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  63859 MW;  E7D90E166F1EF02D CRC64;
     MAATIKWWQQ AVVYQVYPRS FQDTNHDGIG DLKGITAHLD YLKQLGIDVI WLNPIYRSPN
     DDNGYDISDY QQIAADFGTM ADFDELLQAA HDRGLKIIMD LVVNHTSDEH PRFKRSRQDR
     TNQYRDFYFW RSGNGKKAPN NWEAAFGGSA WQYDEQTQQY YLHTFSTKQP DLNWENPTLR
     ESVYTMMTWW LNKGVDGFRM DVINQISKLP GLPDGPLKPH SQFGDARVTN GPRVHEFLQE
     MNQEVLSQFD IMTVGETHGV TPADALKYAG ADQHELDMVF EFQHLRLDNS QHGLGKWSTR
     KTPLVALKKV ISDWQVGLEG RAWNSLFWNN HDTPRAVSRF GDDRPAYRVR SAKMLATCLH
     LLQGTPYIYQ GEELGMTDAH FTELASYRDI ESLSAYRDLV TERQLLSPAD MMARLAAASR
     DNSRTPMQWD TEVNAGFSDA APWLTVNPNY RQINAAAALA DPDSVWYYYQ HLIQLRHQYP
     SVTLGSFELL WADDPQYSYM HGNGKADLAS LLQFHSRDTV PTTGSISDPT AKCLISNYGE
     QQPNKLRPYE AWVYQLA