ID   AGL2_BACTQ              Reviewed;         787 AA.
AC   Q9F234;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Alpha-glucosidase 2;
DE            EC=3.2.1.20;
DE   AltName: Full=Alpha-glucosidase II;
OS   Bacillus thermoamyloliquefaciens.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KP1071;
RX   PubMed=10945254; DOI=10.1271/bbb.64.1379;
RA   Kashiwabara S., Azuma S., Tsuduki M., Suzuki Y.;
RT   "The primary structure of the subunit in Bacillus thermoamyloliquefaciens
RT   KP1071 molecular weight 540,000 homohexameric alpha-glucosidase II
RT   belonging to the glycosyl hydrolase family 31.";
RL   Biosci. Biotechnol. Biochem. 64:1379-1393(2000).
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   -!- SUBUNIT: Homohexamer.
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; AB012238; BAA76396.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F234; -.
DR   SMR; Q9F234; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   BRENDA; 3.2.1.20; 7482.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR032513; AGL_N.
DR   InterPro; IPR033403; DUF5110.
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; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16338; DUF4968; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 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   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..787
FT                   /note="Alpha-glucosidase 2"
FT                   /id="PRO_0000185368"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        484
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   787 AA;  91072 MW;  6BDD837E2C3304BF CRC64;
     MLEDTSFAIQ PEQDDKTQET HRIDIGNMHT FSHTEHVFSF HCDTGIVKIR FYREDIVRIA
     FNPFGETSLS TSVAVVKEPE KVDASVHETE EEVTLTSAKQ TVVLQKRPFR VRIYDNHGRL
     LVAEGKKGMA FTYQGEVCCF KMMDEADHFY GFGEKTGFLD KRGETMTMWN TDVYAPHNPE
     TDPLYQSHPY FMTVRNGSAH GIFFDNTYKT TFDFQTATDE YCFSAEGGAI DYYVFAGPTP
     KDVLEQYTDL TGRMPLPPKW ALGYHQSRYS YETEQEVREI AQTFIEKDIP LDVIYLDIHY
     MNGYRVFTFD RNRFPNLKQL IADLKQKGIR VVPIVDPGVK EDPEYVIYQE GIRHDYFCKY
     IEGNVYFGEV WPGKSAFPDF TNKKVRKWWG EKHQFYTDLG IEGIWNDMNE PSVFNETKTM
     DVKVIHDNDG DPKTHRELHN VYGFMMGEAT YKGMKKLLNG KRPFLLTRAG FSGIQRYAAV
     WTGDNRSFWE HLQMSLPMCM NLGLSGVAFC GPDVGGFAHN TNGELLTRWM QVGAFTPYFR
     NHCAIGFRRQ EPWAFGEKYE RIIKKYIRLR YQWLPHLYTL FAEAHETGAP VMRPLFFEYP
     DDENTYNLYD EFLVGANVLI APIMTPSTTR RVAYFPKGNW VDYWTGEVLE GGQYHLISAD
     LETLPIFIKQ GSAIALGDVK RSTEMPDEHR TVHIYKANGG KATYVLYDDD GQTFSYEKGD
     YLRMYIEVEY GENSVHIVTK SEGTYQPSWK LSFAIHHATE QTKVTIDGNE QNAIFDPHQR
     ILLIQSE