O16G2_BACSU
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 03-AUG-2022, entry version 126.
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; Firmicutes; 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}.
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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; O34364; -.
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 OMA; YSTARDV; -.
DR PhylomeDB; O34364; -.
DR BioCyc; BSUB:BSU02840-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: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; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 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