ID   O16G_BACF5              Reviewed;         509 AA.
AC   P29093;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-MAY-2023, entry version 96.
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   Bacillus sp. (strain F5).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=268806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RA   Yamamoto M., Horikoshi K.;
RT   "Nucleotide sequence of alkalophilic Bacillus oligo-1,6-glucosidase gene
RT   and the properties of the gene product in Escherichia coli HB101.";
RL   Denpun Kagaku 37:137-144(1990).
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; D00638; BAA00534.1; -; Genomic_DNA.
DR   PIR; JQ0535; JQ0535.
DR   AlphaFoldDB; P29093; -.
DR   SMR; P29093; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF184; OLIGO-1,6-GLUCOSIDASE 1; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..509
FT                   /note="Oligo-1,6-glucosidase"
FT                   /id="PRO_0000054316"
FT   ACT_SITE        198
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            331
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  59909 MW;  0D1880055B35F692 CRC64;
     MSQWWKEAVV YQIYPRSFYD SNGDGFGDLQ GVIQKLDYIK RLGADVIWLC PVFDSPQDDN
     GYDISDYRSI YEKFGTNDDM FQLIDEVHKR GMKIIMDLVV NHSSDEHAWF AESRKSKDNP
     YRDYYFWKDP KADGSEPNNW GAIFSGPAWS AMSTAQYYLH YFSKKQPDLN WENEAVRREV
     YDLMTFWMDR GVDGWRMDVI GSISKFVDFP DYETDDSRPY VVGRYHSNGP RLHEFIQEMN
     REVLSRYDCM TVGEAGGSDV EEAKKYTDPS RHELNMIFTF EHMDIDTKQH SPNGKWQMKP
     FDPIALKKTM TRWQTALMNV GWNTLYFENH DQPRVISAGA MTRELRKQSR QSISNSSARH
     EGNPFIYQGE EIGMTNSEMP LEMYDDLEIK NAYRELVIEN KTMTEEDFRK AVAKKGRDHA
     RTPMQWDDGK YAGFTDGEAW LAVNPRYQEI NVKESLADED SIFYYYQKLI GLRKQNKVIV
     YGDYRLLLEE DPRIFAYIRE YRGEKLLVP
//