ID   O16G_PARTM              Reviewed;         562 AA.
AC   P29094;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-MAY-2023, entry version 108.
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   Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=1426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, AND
RP   TEMPERATURE DEPENDENCE.
RC   STRAIN=ATCC 43742 / DSM 2542 / NCIMB 11955 / NRRL B-14516 / KP 1006;
RX   PubMed=1761534; DOI=10.1016/s0021-9258(18)54226-5;
RA   Watanabe K., Chishiro K., Kitamura K., Suzuki Y.;
RT   "Proline residues responsible for thermostability occur with high frequency
RT   in the loop regions of an extremely thermostable oligo-1,6-glucosidase from
RT   Bacillus thermoglucosidasius KP1006.";
RL   J. Biol. Chem. 266:24287-24294(1991).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Extremely thermostable. {ECO:0000269|PubMed:1761534};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; D10487; BAA01368.1; -; Genomic_DNA.
DR   PIR; A41707; A41707.
DR   AlphaFoldDB; P29094; -.
DR   SMR; P29094; -.
DR   STRING; 1426.AOT13_06350; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   eggNOG; COG0366; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Calcium; Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Metal-binding.
FT   CHAIN           1..562
FT                   /note="Oligo-1,6-glucosidase"
FT                   /id="PRO_0000054318"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O06994"
FT   BINDING         23
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O06994"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O06994"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O06994"
FT   SITE            330
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  66505 MW;  925EB5924726D42A CRC64;
     MERVWWKEAV VYQIYPRSFY DSNGDGIGDI RGIIAKLDYL KELGVDVVWL SPVYKSPNDD
     NGYDISDYRD IMDEFGTMAD WKTMLEEMHK RGIKLVMDLV VNHTSDEHPW FIESRKSKDN
     PYRDYYIWRP GKNGKEPNNW ESVFSGSAWE YDEMTGEYYL HLFSKKQPDL NWENPKVRRE
     VYEMMKFWLD KGVDGFRMDV INMISKVPEL PDGEPQSGKK YASGSRYYMN GPRVHEFLQE
     MNREVLSKYD IMTVGETPGV TPKEGILYTD PSRRELNMVF QFEHMDLDSG PGGKWDIRPW
     SLADLKKTMT KWQKELEGKG WNSLYLNNHD QPRAVSRFGD DGKYRVESAK MLATFLHMMQ
     GTPYIYQGEE IGMTNVRFPS IEDYRDIETL NMYKERVEEY GEDPQEVMEK IYYKGRDNAR
     TPMQWDDSEN AGFTAGTPWI PVNPNYKEIN VKAALEDPNS VFHYYKKLIQ LRKQHDIIVY
     GTYDLILEDD PYIYRYTRTL GNEQLIVITN FSEKTPVFRL PDHIIYKTKE LLISNYDVDE
     AEELKEIRLR PWEARVYKIR LP
//