ID   O16G_WEICA              Reviewed;         555 AA.
AC   Q45101;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Oligo-1,6-glucosidase;
DE            EC=3.2.1.10;
DE   AltName: Full=Dextrin 6-alpha-D-glucanohydrolase;
DE   AltName: Full=Oligosaccharide alpha-1,6-glucosidase;
DE   AltName: Full=Sucrase-isomaltase;
DE            Short=Isomaltase;
GN   Name=malL;
OS   Weizmannia coagulans (Bacillus coagulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Weizmannia.
OX   NCBI_TaxID=1398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7050 / DSM 1 / JCM 2257 / CCUG 7417 / NBRC 12583 / NCIMB 9365 /
RC   NCTC 10334 / NRS 609;
RX   PubMed=8787404; DOI=10.1128/aem.62.6.2066-2073.1996;
RA   Watanabe K., Kitamura K., Suzuki Y.;
RT   "Analysis of the critical sites for protein thermostabilization by proline
RT   substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and
RT   the evolutionary consideration of proline residues.";
RL   Appl. Environ. Microbiol. 62:2066-2073(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC         oligosaccharides produced from starch and glycogen by alpha-amylase,
CC         and in isomaltose.; EC=3.2.1.10;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; D78342; BAA11354.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q45101; -.
DR   SMR; Q45101; -.
DR   STRING; 1398.AB434_0896; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q45101; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004574; F:oligo-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..555
FT                   /note="Oligo-1,6-glucosidase"
FT                   /id="PRO_0000054314"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            332
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  64991 MW;  CE2BB1D7B4E226D8 CRC64;
     MTEWWKKAVV YQIYPRSFYD TNGDGIGDLR GIMDKLDYLK TLGIDCIWIS PVYDSPQDDN
     GYDIRDYRKI DKMFGTNEDM DRLLDEAHAR GIKIVMDLVV NHTSDEHAWF VESRKSKDNP
     YRDFYFWKDP KPDGTPPNNW GSMFSGSAWE YDETTGQYYL HYFSKKQPDL NWENEKVRKE
     IYDMMKFWMD KGVDGWRMDV IGSISKFLDF PDYELPEGQK YGIGKYHANG PRLHAFIQEM
     NREVLSKYDC MTVGEAIGSD VEIARKYTGP DRHELNMIFN FEHMDVDTKP GSPAGKWALK
     PFDLVELKQI LSRWQYELAD TGWNALYFEN HDQARVVSRW GNDTTYRAEC AKAFATILHG
     LKGTPFIYQG EEIGMVNADL ELEEYDDIEI RNAYQELVME NQIMSKDEFL TAVRKKGRDN
     ARTPMQWDGS FNAGFTTGTP WLKVNSRYSE INVAKALQEP DSIFYYYQSL IKLRHSYDVF
     TDGRYELLMP DHPHLYVYTR ENESEKLLVA ANLSENTVSF DQPDDNWKLL LGNYEDTGTS
     TLFRPYEAAI YYLEK