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P29094 (O16G_GEOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 76. 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
OrganismGeobacillus thermoglucosidasius (Bacillus thermoglucosidasius)
Taxonomic identifier1426 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length562 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.

Biophysicochemical properties

Temperature dependence:

Extremely thermostable.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect 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 – 562562Oligo-1,6-glucosidase
PRO_0000054318

Sites

Active site1991Nucleophile By similarity
Active site2561Proton donor By similarity
Site3301Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P29094 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 925EB5924726D42A

FASTA56266,505
        10         20         30         40         50         60 
MERVWWKEAV VYQIYPRSFY DSNGDGIGDI RGIIAKLDYL KELGVDVVWL SPVYKSPNDD 

        70         80         90        100        110        120 
NGYDISDYRD IMDEFGTMAD WKTMLEEMHK RGIKLVMDLV VNHTSDEHPW FIESRKSKDN 

       130        140        150        160        170        180 
PYRDYYIWRP GKNGKEPNNW ESVFSGSAWE YDEMTGEYYL HLFSKKQPDL NWENPKVRRE 

       190        200        210        220        230        240 
VYEMMKFWLD KGVDGFRMDV INMISKVPEL PDGEPQSGKK YASGSRYYMN GPRVHEFLQE 

       250        260        270        280        290        300 
MNREVLSKYD IMTVGETPGV TPKEGILYTD PSRRELNMVF QFEHMDLDSG PGGKWDIRPW 

       310        320        330        340        350        360 
SLADLKKTMT KWQKELEGKG WNSLYLNNHD QPRAVSRFGD DGKYRVESAK MLATFLHMMQ 

       370        380        390        400        410        420 
GTPYIYQGEE IGMTNVRFPS IEDYRDIETL NMYKERVEEY GEDPQEVMEK IYYKGRDNAR 

       430        440        450        460        470        480 
TPMQWDDSEN AGFTAGTPWI PVNPNYKEIN VKAALEDPNS VFHYYKKLIQ LRKQHDIIVY 

       490        500        510        520        530        540 
GTYDLILEDD PYIYRYTRTL GNEQLIVITN FSEKTPVFRL PDHIIYKTKE LLISNYDVDE 

       550        560 
AEELKEIRLR PWEARVYKIR LP 

« Hide

References

[1]"Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006."
Watanabe K., Chishiro K., Kitamura K., Suzuki Y.
J. Biol. Chem. 266:24287-24294(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, TEMPERATURE DEPENDENCE.
Strain: KP1006.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10487 Genomic DNA. Translation: BAA01368.1.
PIRA41707.

3D structure databases

ProteinModelPortalP29094.
SMRP29094. Positions 1-560.
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.
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 nameO16G_GEOTM
AccessionPrimary (citable) accession number: P29094
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 11, 2013
This is version 76 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