ID O16G2_BACSU Reviewed; 561 AA. AC O34364; Q797R7; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Probable oligo-1,6-glucosidase 2; DE EC=3.2.1.10; DE AltName: Full=Oligosaccharide alpha-1,6-glucosidase 2; DE AltName: Full=Sucrase-isomaltase 2; DE Short=Isomaltase 2; GN Name=ycdG; OrderedLocusNames=BSU02840; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9274031; DOI=10.1099/00221287-143-8-2775; RA Kumano M., Tamakoshi A., Yamane K.; RT "A 32 kb nucleotide sequence from the region of the lincomycin-resistance RT gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and RT identification of the site of the lin-2 mutation."; RL Microbiology 143:2775-2782(1997). 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 INDUCTION. RX PubMed=11544224; DOI=10.1128/jb.183.19.5617-5631.2001; RA Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.; RT "Global analysis of the general stress response of Bacillus subtilis."; RL J. Bacteriol. 183:5617-5631(2001). 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 {ECO:0000250}. CC -!- INDUCTION: By ethanol, heat and salt via sigma B-dependent promoter. CC {ECO:0000269|PubMed:11544224}. 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; AB000617; BAA22245.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12078.1; -; Genomic_DNA. DR PIR; H69755; H69755. DR RefSeq; NP_388166.1; NC_000964.3. DR RefSeq; WP_003234736.1; NZ_JNCM01000030.1. DR AlphaFoldDB; O34364; -. DR SMR; O34364; -. DR STRING; 224308.BSU02840; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 224308-BSU02840; -. DR EnsemblBacteria; CAB12078; CAB12078; BSU_02840. DR GeneID; 938375; -. DR KEGG; bsu:BSU02840; -. DR PATRIC; fig|224308.179.peg.295; -. DR eggNOG; COG0366; Bacteria. DR InParanoid; O34364; -. DR OrthoDB; 9805159at2; -. DR PhylomeDB; O34364; -. DR BioCyc; BSUB:BSU02840-MONOMER; -. 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:0004574; F:oligo-1,6-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central. 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 2: Evidence at transcript level; KW Cytoplasm; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1..561 FT /note="Probable oligo-1,6-glucosidase 2" FT /id="PRO_0000360818" FT ACT_SITE 199 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 255 FT /note="Proton donor" FT /evidence="ECO:0000250" FT SITE 330 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 561 AA; 65816 MW; 1E879220CAE04BBF CRC64; MKTDWWKDAV VYQIYPRSFQ DSNGDGIGDL RGIISRLDYI KELGADVIWI CPIYPSPNVD YGYDVTNHKA IMDSYGTMDD FHELLDQVHQ RGLKLVMDFV LNHTSVEHPW FKEAELDKNS KYRSYYYWRP GTKNGPPTDW LSNYGCPVWQ YEEHTGEYYL HMNAVKQADL NWENPEVRQA VYDMMKFWLD KGVDGLRIDQ LHLISKKEYL PSYEDYINQQ AEPKPFQPNG ERIHDYLKEI TDEVFSHYDV MSVGEVGSVT PEEGLKYTGT DKHELNMIFH FQHMELDQQP GKEHWDLKPL ELSDLKSVLT KWQKKLEHQG WNTLFWCNHD QPRIVSRFGD DGEYRKASAK MLAAVIYFMK GTPYIYQGEE IGMTNAPFTR IEDYKDIQTI NMYHKRVFEK GYDPNDVMRS ILAKSRDHAR TPMQWNSGKN AGFTDGTPWL KVNPNFTAIN VEEAQGDPDS VLNYYKKLIS LRKQYADLMK GSFDLLLPDD PQLFVYMREN SKQQLLSVNN FSKEQAVFQW PKNCGKAQAS LLLSNYNNDD LDDEMVFRPY ESRVYLLDKT N //