ID O16G_BACCE Reviewed; 558 AA. AC P21332; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 24-JAN-2024, entry version 123. 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 cereus. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=ATCC 7064 / NRS 201; RX PubMed=2120057; DOI=10.1111/j.1432-1033.1990.tb19267.x; RA Watanabe K., Kitamura K., Iha H., Suzuki Y.; RT "Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 RT deduced from the nucleotide sequence of the cloned gene."; RL Eur. J. Biochem. 192:609-620(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RC STRAIN=ATCC 7064 / NRS 201; RX PubMed=8370659; DOI=10.1093/oxfordjournals.jbchem.a124097; RA Kizaki H., Hata Y., Watanabe K., Katsube Y., Suzuki Y.; RT "Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase RT revealed by 3.0-A resolution X-ray analysis."; RL J. Biochem. 113:646-649(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=ATCC 7064 / NRS 201; RX PubMed=9193006; DOI=10.1006/jmbi.1997.1018; RA Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y.; RT "The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at RT 2.0-A resolution: structural characterization of proline-substitution sites RT for protein thermostabilization."; RL J. Mol. Biol. 269:142-153(1997). 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}. 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; X53507; CAA37583.1; -; Genomic_DNA. DR PIR; S13579; S13579. DR RefSeq; WP_000415199.1; NZ_PHQW02000012.1. DR PDB; 1UOK; X-ray; 2.00 A; A=1-558. DR PDBsum; 1UOK; -. DR AlphaFoldDB; P21332; -. DR SMR; P21332; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR eggNOG; COG0366; Bacteria. DR SABIO-RK; P21332; -. DR EvolutionaryTrace; P21332; -. 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; IPR032091; Malt_amylase_C. 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 Pfam; PF16657; Malt_amylase_C; 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 3D-structure; Calcium; Cytoplasm; Direct protein sequencing; Glycosidase; KW Hydrolase; Metal-binding. FT CHAIN 1..558 FT /note="Oligo-1,6-glucosidase" FT /id="PRO_0000054313" FT ACT_SITE 199 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 255 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 329 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT HELIX 5..8 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 22..27 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 30..34 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 37..43 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:1UOK" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 78..90 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:1UOK" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 175..190 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:1UOK" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 233..243 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 251..255 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 261..268 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 301..314 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 333..336 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 344..356 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 358..365 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 386..397 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 403..413 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:1UOK" FT TURN 428..431 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 443..446 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 450..455 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 460..473 FT /evidence="ECO:0007829|PDB:1UOK" FT HELIX 475..479 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 481..486 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 490..499 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 502..509 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 511..513 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 515..518 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 528..535 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 543..547 FT /evidence="ECO:0007829|PDB:1UOK" FT STRAND 552..557 FT /evidence="ECO:0007829|PDB:1UOK" SQ SEQUENCE 558 AA; 66013 MW; 502336D7A77C7182 CRC64; MEKQWWKESV VYQIYPRSFM DSNGDGIGDL RGIISKLDYL KELGIDVIWL SPVYESPNDD NGYDISDYCK IMNEFGTMED WDELLHEMHE RNMKLMMDLV VNHTSDEHNW FIESRKSKDN KYRDYYIWRP GKEGKEPNNW GAAFSGSAWQ YDEMTDEYYL HLFSKKQPDL NWDNEKVRQD VYEMMKFWLE KGIDGFRMDV INFISKEEGL PTVETEEEGY VSGHKHFMNG PNIHKYLHEM NEEVLSHYDI MTVGEMPGVT TEEAKLYTGE ERKELQMVFQ FEHMDLDSGE GGKWDVKPCS LLTLKENLTK WQKALEHTGW NSLYWNNHDQ PRVVSRFGND GMYRIESAKM LATVLHMMKG TPYIYQGEEI GMTNVRFESI DEYRDIETLN MYKEKVMERG EDIEKVMQSI YIKGRDNART PMQWDDQNHA GFTTGEPWIT VNPNYKEINV KQAIQNKDSI FYYYKKLIEL RKNNEIVVYG SYDLILENNP SIFAYVRTYG VEKLLVIANF TAEECIFELP EDISYSEVEL LIHNYDVENG PIENITLRPY EAMVFKLK //