O16G1_BACSU
ID O16G1_BACSU Reviewed; 561 AA.
AC O06994;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Oligo-1,6-glucosidase 1;
DE EC=3.2.1.10 {ECO:0000269|PubMed:10229946, ECO:0000269|PubMed:24015933, ECO:0000269|PubMed:9573215};
DE AltName: Full=Dextrin 6-alpha-D-glucanohydrolase;
DE AltName: Full=Oligosaccharide alpha-1,6-glucosidase 1;
DE AltName: Full=Sucrase-isomaltase 1;
DE Short=Isomaltase 1;
GN Name=malL; Synonyms=yvdL; OrderedLocusNames=BSU34560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RX PubMed=9573215; DOI=10.1128/jb.180.9.2574-2578.1998;
RA Schoenert S., Buder T., Dahl M.K.;
RT "Identification and enzymatic characterization of the maltose-inducible
RT alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis.";
RL J. Bacteriol. 180:2574-2578(1998).
RN [4]
RP CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10229946; DOI=10.1016/s0923-2508(99)80033-3;
RA Schoenert S., Buder T., Dahl M.K.;
RT "Properties of maltose-inducible alpha-glucosidase MalL (sucrase-
RT isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to
RT maltodextrin utilization.";
RL Res. Microbiol. 150:167-177(1999).
RN [5] {ECO:0007744|PDB:4M56, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MAZ, ECO:0007744|PDB:4MB1}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND
RP CATALYTIC ACTIVITY.
RX PubMed=24015933; DOI=10.1021/cb4005029;
RA Hobbs J.K., Jiao W., Easter A.D., Parker E.J., Schipper L.A., Arcus V.L.;
RT "Change in heat capacity for enzyme catalysis determines temperature
RT dependence of enzyme catalyzed rates.";
RL ACS Chem. Biol. 8:2388-2393(2013).
CC -!- FUNCTION: Hydrolyzes various disaccharides such as sucrose, maltose,
CC and isomaltose with different efficiencies. Also hydrolyzes longer
CC maltodextrins from maltotriose up to maltohexaose, but not
CC maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
CC {ECO:0000269|PubMed:10229946}.
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 Evidence={ECO:0000269|PubMed:10229946, ECO:0000269|PubMed:24015933,
CC ECO:0000269|PubMed:9573215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:10229946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; Z94043; CAB08041.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15461.1; -; Genomic_DNA.
DR PIR; D70034; D70034.
DR RefSeq; NP_391336.1; NC_000964.3.
DR RefSeq; WP_003243333.1; NZ_JNCM01000033.1.
DR PDB; 4M56; X-ray; 2.30 A; A/B=1-561.
DR PDB; 4M8U; X-ray; 1.45 A; A=1-561.
DR PDB; 4MAZ; X-ray; 1.60 A; A=1-561.
DR PDB; 4MB1; X-ray; 1.40 A; A=1-561.
DR PDB; 5WCZ; X-ray; 1.58 A; A/B=1-561.
DR PDB; 7LV6; X-ray; 1.10 A; B=3-561.
DR PDBsum; 4M56; -.
DR PDBsum; 4M8U; -.
DR PDBsum; 4MAZ; -.
DR PDBsum; 4MB1; -.
DR PDBsum; 5WCZ; -.
DR PDBsum; 7LV6; -.
DR AlphaFoldDB; O06994; -.
DR SMR; O06994; -.
DR STRING; 224308.BSU34560; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O06994; -.
DR PRIDE; O06994; -.
DR EnsemblBacteria; CAB15461; CAB15461; BSU_34560.
DR GeneID; 938623; -.
DR KEGG; bsu:BSU34560; -.
DR PATRIC; fig|224308.179.peg.3743; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; O06994; -.
DR OMA; WNQPEVH; -.
DR PhylomeDB; O06994; -.
DR BioCyc; BSUB:BSU34560-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
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:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..561
FT /note="Oligo-1,6-glucosidase 1"
FT /id="PRO_0000054317"
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 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24015933,
FT ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24015933,
FT ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24015933,
FT ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24015933,
FT ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24015933,
FT ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5WCZ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4M8U"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:4MB1"
FT TURN 446..450
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 463..476
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 493..502
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:4MB1"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:4MB1"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:4MB1"
SQ SEQUENCE 561 AA; 66081 MW; 2B43E9A4AD65A222 CRC64;
MSEWWKEAVV YQIYPRSFYD ANGDGFGDLQ GVIQKLDYIK NLGADVIWLS PVFDSPQDDN
GYDISDYKNM YEKFGTNEDM FQLIDEVHKR GMKIVMDLVV NHTSDEHAWF AESRKSKDNP
YRDYYLWKDP KPDGSEPNNW GSIFSGSAWT YDEGTGQYYL HYFSKKQPDL NWENEAVRRE
VYDVMRFWMD RGVDGWRMDV IGSISKYTDF PDYETDHSRS YIVGRYHSNG PRLHEFIQEM
NREVLSHYDC MTVGEANGSD IEEAKKYTDA SRQELNMIFT FEHMDIDKEQ NSPNGKWQIK
PFDLIALKKT MTRWQTGLMN VGWNTLYFEN HDQPRVISRW GNDRKLRKEC AKAFATVLHG
MKGTPFIYQG EEIGMVNSDM PLEMYDDLEI KNAYRELVVE NKTMSEKEFV KAVMIKGRDH
ARTPMQWDAG KHAGFTAGDP WIPVNSRYQD INVKESLEDQ DSIFFYYQKL IQLRKQYKIM
IYGDYQLLQE NDPQVFSYLR EYRGEKLLVV VNLSEEKALF EAPPELIHER WKVLISNYPQ
ERADLKSISL KPYEAVMGIS I
