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P21332 (O16G_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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:
Oligo-1,6-glucosidase

EC=3.2.1.10
Alternative name(s):
Dextrin 6-alpha-D-glucanohydrolase
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Short name=Isomaltase
Gene names
Name:malL
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
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 – 558558Oligo-1,6-glucosidase
PRO_0000054313

Sites

Active site1991Nucleophile
Active site2551Proton donor
Site3291Transition state stabilizer By similarity

Secondary structure

........................................................................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21332 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 502336D7A77C7182

FASTA55866,013
        10         20         30         40         50         60 
MEKQWWKESV VYQIYPRSFM DSNGDGIGDL RGIISKLDYL KELGIDVIWL SPVYESPNDD 

        70         80         90        100        110        120 
NGYDISDYCK IMNEFGTMED WDELLHEMHE RNMKLMMDLV VNHTSDEHNW FIESRKSKDN 

       130        140        150        160        170        180 
KYRDYYIWRP GKEGKEPNNW GAAFSGSAWQ YDEMTDEYYL HLFSKKQPDL NWDNEKVRQD 

       190        200        210        220        230        240 
VYEMMKFWLE KGIDGFRMDV INFISKEEGL PTVETEEEGY VSGHKHFMNG PNIHKYLHEM 

       250        260        270        280        290        300 
NEEVLSHYDI MTVGEMPGVT TEEAKLYTGE ERKELQMVFQ FEHMDLDSGE GGKWDVKPCS 

       310        320        330        340        350        360 
LLTLKENLTK WQKALEHTGW NSLYWNNHDQ PRVVSRFGND GMYRIESAKM LATVLHMMKG 

       370        380        390        400        410        420 
TPYIYQGEEI GMTNVRFESI DEYRDIETLN MYKEKVMERG EDIEKVMQSI YIKGRDNART 

       430        440        450        460        470        480 
PMQWDDQNHA GFTTGEPWIT VNPNYKEINV KQAIQNKDSI FYYYKKLIEL RKNNEIVVYG 

       490        500        510        520        530        540 
SYDLILENNP SIFAYVRTYG VEKLLVIANF TAEECIFELP EDISYSEVEL LIHNYDVENG 

       550 
PIENITLRPY EAMVFKLK 

« Hide

References

[1]"Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene."
Watanabe K., Kitamura K., Iha H., Suzuki Y.
Eur. J. Biochem. 192:609-620(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: ATCC 7064 / NRS 201.
[2]"Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0-A resolution X-ray analysis."
Kizaki H., Hata Y., Watanabe K., Katsube Y., Suzuki Y.
J. Biochem. 113:646-649(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Strain: ATCC 7064 / NRS 201.
[3]"The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0-A resolution: structural characterization of proline-substitution sites for protein thermostabilization."
Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y.
J. Mol. Biol. 269:142-153(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: ATCC 7064 / NRS 201.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53507 Genomic DNA. Translation: CAA37583.1.
PIRS13579.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UOKX-ray2.00A1-558[»]
ProteinModelPortalP21332.
SMRP21332. Positions 1-558.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-3340-MONOMER.
SABIO-RKP21332.

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...

Other

EvolutionaryTraceP21332.

Entry information

Entry nameO16G_BACCE
AccessionPrimary (citable) accession number: P21332
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries