ID   O16G_ALKHC              Reviewed;         561 AA.
AC   Q9K8U9;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
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; OrderedLocusNames=BH2903;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06622.1; -; Genomic_DNA.
DR   PIR; G84012; G84012.
DR   RefSeq; WP_010899050.1; NC_002570.2.
DR   AlphaFoldDB; Q9K8U9; -.
DR   SMR; Q9K8U9; -.
DR   STRING; 272558.10175525; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAB06622; BAB06622; BAB06622.
DR   KEGG; bha:BH2903; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_1_2_9; -.
DR   OMA; YSTARDV; -.
DR   OrthoDB; 1573900at2; -.
DR   Proteomes; UP000001258; Chromosome.
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; Reference proteome.
FT   CHAIN           1..561
FT                   /note="Oligo-1,6-glucosidase"
FT                   /id="PRO_0000054315"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            330
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   561 AA;  65430 MW;  82C6F3E09F18D4F7 CRC64;
     MSTQWWKESV VYQIYPRSFQ DYNGDGIGDI PGIISRLDYL KTLGVDVIWL SPVYDSPNDD
     NGYDIRDYKA IMDEFGTMAD WETLLAEIHT RGMKLIMDLV VNHSSDEHAW FVESRKSKDN
     PYRDFYIWRP GKDGKEPNNW ASNFSGSAWT YDETTGEYYL HLFSKKQPDL NWENPKLREK
     IYEMMTWWLD KGIDGFRMDV INFISKVDGL PDAEPQPGQP YVSGSNYFMN GPNIHTYLQE
     MHENVLQHYD LMTVGEMPGV TLELAQLYTG EERNELNMVF QFEHVGLDQG PNGKWDLKPL
     ELKDLKASLS RWQKGLQDIG WNSLYWNNHD QPRIVSRFGD DQSYRVESAK MLATLLHCMK
     GTPFIYQGEE IGMTNVRFDS IEQYQDIETL NMYKEKRAQG VPHETLMASI HAKGRDNART
     PMQWDETKHG GFTDGTPWLE VNPNYKEINV KQALKDPNSI FYHYQKLIQL RKEHAILVHG
     SYDLILEDDP EIFAYKRTYN GQTLLVVCNF YGRITDFECP AEVVLSEPTL LLSNYDEEEN
     GSYTSFRLRP YEARVYLGKN E