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O34364 (O16G2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable oligo-1,6-glucosidase 2

EC=3.2.1.10
Alternative name(s):
Oligosaccharide alpha-1,6-glucosidase 2
Sucrase-isomaltase 2
Short name=Isomaltase 2
Gene names
Name:ycdG
Ordered Locus Names:BSU02840
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

Subcellular location

Cytoplasm By similarity.

Induction

By ethanol, heat and salt via sigma B-dependent promoter. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncation binding

Inferred from electronic annotation. Source: InterPro

oligo-1,6-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Probable oligo-1,6-glucosidase 2
PRO_0000360818

Sites

Active site1991Nucleophile By similarity
Active site2551Proton donor By similarity
Site3301Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
O34364 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1E879220CAE04BBF

FASTA56165,816
        10         20         30         40         50         60 
MKTDWWKDAV VYQIYPRSFQ DSNGDGIGDL RGIISRLDYI KELGADVIWI CPIYPSPNVD 

        70         80         90        100        110        120 
YGYDVTNHKA IMDSYGTMDD FHELLDQVHQ RGLKLVMDFV LNHTSVEHPW FKEAELDKNS 

       130        140        150        160        170        180 
KYRSYYYWRP GTKNGPPTDW LSNYGCPVWQ YEEHTGEYYL HMNAVKQADL NWENPEVRQA 

       190        200        210        220        230        240 
VYDMMKFWLD KGVDGLRIDQ LHLISKKEYL PSYEDYINQQ AEPKPFQPNG ERIHDYLKEI 

       250        260        270        280        290        300 
TDEVFSHYDV MSVGEVGSVT PEEGLKYTGT DKHELNMIFH FQHMELDQQP GKEHWDLKPL 

       310        320        330        340        350        360 
ELSDLKSVLT KWQKKLEHQG WNTLFWCNHD QPRIVSRFGD DGEYRKASAK MLAAVIYFMK 

       370        380        390        400        410        420 
GTPYIYQGEE IGMTNAPFTR IEDYKDIQTI NMYHKRVFEK GYDPNDVMRS ILAKSRDHAR 

       430        440        450        460        470        480 
TPMQWNSGKN AGFTDGTPWL KVNPNFTAIN VEEAQGDPDS VLNYYKKLIS LRKQYADLMK 

       490        500        510        520        530        540 
GSFDLLLPDD PQLFVYMREN SKQQLLSVNN FSKEQAVFQW PKNCGKAQAS LLLSNYNNDD 

       550        560 
LDDEMVFRPY ESRVYLLDKT N 

« Hide

References

« Hide 'large scale' references
[1]"A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation."
Kumano M., Tamakoshi A., Yamane K.
Microbiology 143:2775-2782(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Global analysis of the general stress response of Bacillus subtilis."
Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.
J. Bacteriol. 183:5617-5631(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000617 Genomic DNA. Translation: BAA22245.1.
AL009126 Genomic DNA. Translation: CAB12078.1.
PIRH69755.
RefSeqNP_388166.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34364.
SMRO34364. Positions 1-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU02840.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbO34364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12078; CAB12078; BSU02840.
GeneID938375.
KEGGbsu:BSU02840.
PATRIC18972127. VBIBacSub10457_0292.

Organism-specific databases

GenoListBSU02840.

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000220641.
KOK01182.
OMAEERNDQT.
OrthoDBEOG6RVFV2.
PhylomeDBO34364.

Enzyme and pathway databases

BioCycBSUB:BSU02840-MONOMER.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameO16G2_BACSU
AccessionPrimary (citable) accession number: O34364
Secondary accession number(s): Q797R7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList