O16G_BACCE
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 03-AUG-2022, entry version 119.
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; Firmicutes; 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}.
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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 STRING; 1396.DJ87_845; -.
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 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 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
