ID   O16G3_BACSU             Reviewed;         554 AA.
AC   O05242; Q795N0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Probable oligo-1,6-glucosidase 3;
DE            EC=3.2.1.10;
DE   AltName: Full=Oligosaccharide alpha-1,6-glucosidase 3;
DE   AltName: Full=Sucrase-isomaltase 3;
DE            Short=Isomaltase 3;
GN   Name=yugT; OrderedLocusNames=BSU31290;
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=9274030; DOI=10.1099/00221287-143-8-2769;
RA   Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA   Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT   "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT   of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL   Microbiology 143:2769-2774(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   SEQUENCE REVISION TO 262.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; Z93935; CAB07926.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15118.2; -; Genomic_DNA.
DR   PIR; H70011; H70011.
DR   RefSeq; NP_391007.2; NC_000964.3.
DR   RefSeq; WP_003243842.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O05242; -.
DR   SMR; O05242; -.
DR   STRING; 224308.BSU31290; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 224308-BSU31290; -.
DR   EnsemblBacteria; CAB15118; CAB15118; BSU_31290.
DR   GeneID; 938857; -.
DR   KEGG; bsu:BSU31290; -.
DR   PATRIC; fig|224308.179.peg.3391; -.
DR   eggNOG; COG0366; Bacteria.
DR   InParanoid; O05242; -.
DR   OrthoDB; 9805159at2; -.
DR   PhylomeDB; O05242; -.
DR   BioCyc; BSUB:BSU31290-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; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF178; OLIGO-1,6-GLUCOSIDASE 3-RELATED; 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   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Probable oligo-1,6-glucosidase 3"
FT                   /id="PRO_0000361649"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            326
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        262
FT                   /note="A -> P (in Ref. 1; CAB07926)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  63969 MW;  67AD34910C96B6B7 CRC64;
     MKKAWWKEAV VYQIYPRSFK DSNGDGIGDI QGIRTKLSYI KELGADVIWI CPLYDSPNAD
     NGYDIRDYQN ILSEFGTMED FDELLGDIHD LDMKLIMDLV VNHTSDEHPW FIESRSSIHS
     EKRDWYIWKD GKNGKTPNNW ESIFGGPAWE YDQKTSQYYL HLFDKKQPDL NWENEKVRNA
     VYDMINWWLD KGIDGFRVDA ITHIKKKEGF PDMPNPKGLD YVPSFPYHMN ADGIMDLLTE
     LKENTFSRYP IMTVGEANGV AAKEAADWAG EKNGIFSMIF QFEHLGLWDV EINESIDIVA
     FKRILTDWQD SLEGIGWNAL FMENHDQPRS VSVWGDDGVY LKESAKALSA VYFLMKGTPF
     IYQGQELGMT NVAFPSIEDY DDVALKRLYE TKTAKGTSHE DVMKIVWKKG RDNSRTPMQW
     NAGPYAGFSE AKPWIGINEN YKWLNAEAQK NDKTSVYHFY KSLIKLRQTY DVFINGTYEL
     ILPEDQQIFA YLRKNESHTA LIAANLTGTP ALFRHSGLPL SSDALVLSNI ETEPHKHMTS
     VLLKPYEARI YLWC
//