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Q45101 (O16G_BACCO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 coagulans
Taxonomic identifier1398 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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
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 – 555555Oligo-1,6-glucosidase
PRO_0000054314

Sites

Active site1991Nucleophile By similarity
Active site2551Proton donor By similarity
Site3321Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q45101 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CE2BB1D7B4E226D8

FASTA55564,991
        10         20         30         40         50         60 
MTEWWKKAVV YQIYPRSFYD TNGDGIGDLR GIMDKLDYLK TLGIDCIWIS PVYDSPQDDN 

        70         80         90        100        110        120 
GYDIRDYRKI DKMFGTNEDM DRLLDEAHAR GIKIVMDLVV NHTSDEHAWF VESRKSKDNP 

       130        140        150        160        170        180 
YRDFYFWKDP KPDGTPPNNW GSMFSGSAWE YDETTGQYYL HYFSKKQPDL NWENEKVRKE 

       190        200        210        220        230        240 
IYDMMKFWMD KGVDGWRMDV IGSISKFLDF PDYELPEGQK YGIGKYHANG PRLHAFIQEM 

       250        260        270        280        290        300 
NREVLSKYDC MTVGEAIGSD VEIARKYTGP DRHELNMIFN FEHMDVDTKP GSPAGKWALK 

       310        320        330        340        350        360 
PFDLVELKQI LSRWQYELAD TGWNALYFEN HDQARVVSRW GNDTTYRAEC AKAFATILHG 

       370        380        390        400        410        420 
LKGTPFIYQG EEIGMVNADL ELEEYDDIEI RNAYQELVME NQIMSKDEFL TAVRKKGRDN 

       430        440        450        460        470        480 
ARTPMQWDGS FNAGFTTGTP WLKVNSRYSE INVAKALQEP DSIFYYYQSL IKLRHSYDVF 

       490        500        510        520        530        540 
TDGRYELLMP DHPHLYVYTR ENESEKLLVA ANLSENTVSF DQPDDNWKLL LGNYEDTGTS 

       550 
TLFRPYEAAI YYLEK 

« Hide

References

[1]"Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues."
Watanabe K., Kitamura K., Suzuki Y.
Appl. Environ. Microbiol. 62:2066-2073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 7050 / DSM 1 / JCM 2257 / NCIB 9365 / NCTC 10334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78342 Genomic DNA. Translation: BAA11354.1.

3D structure databases

ProteinModelPortalQ45101.
SMRQ45101. Positions 2-554.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR022567. DUF3459.
IPR015902. 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.
PF11941. DUF3459. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameO16G_BACCO
AccessionPrimary (citable) accession number: Q45101
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 72 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