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Q9K8U9 (O16G_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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
Ordered Locus Names:BH2903
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length561 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
   Technical termComplete 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 – 561561Oligo-1,6-glucosidase
PRO_0000054315

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9K8U9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 82C6F3E09F18D4F7

FASTA56165,430
        10         20         30         40         50         60 
MSTQWWKESV VYQIYPRSFQ DYNGDGIGDI PGIISRLDYL KTLGVDVIWL SPVYDSPNDD 

        70         80         90        100        110        120 
NGYDIRDYKA IMDEFGTMAD WETLLAEIHT RGMKLIMDLV VNHSSDEHAW FVESRKSKDN 

       130        140        150        160        170        180 
PYRDFYIWRP GKDGKEPNNW ASNFSGSAWT YDETTGEYYL HLFSKKQPDL NWENPKLREK 

       190        200        210        220        230        240 
IYEMMTWWLD KGIDGFRMDV INFISKVDGL PDAEPQPGQP YVSGSNYFMN GPNIHTYLQE 

       250        260        270        280        290        300 
MHENVLQHYD LMTVGEMPGV TLELAQLYTG EERNELNMVF QFEHVGLDQG PNGKWDLKPL 

       310        320        330        340        350        360 
ELKDLKASLS RWQKGLQDIG WNSLYWNNHD QPRIVSRFGD DQSYRVESAK MLATLLHCMK 

       370        380        390        400        410        420 
GTPFIYQGEE IGMTNVRFDS IEQYQDIETL NMYKEKRAQG VPHETLMASI HAKGRDNART 

       430        440        450        460        470        480 
PMQWDETKHG GFTDGTPWLE VNPNYKEINV KQALKDPNSI FYHYQKLIQL RKEHAILVHG 

       490        500        510        520        530        540 
SYDLILEDDP EIFAYKRTYN GQTLLVVCNF YGRITDFECP AEVVLSEPTL LLSNYDEEEN 

       550        560 
GSYTSFRLRP YEARVYLGKN E 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06622.1.
PIRG84012.
RefSeqNP_243769.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K8U9.
SMRQ9K8U9. Positions 1-556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH2903.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06622; BAB06622; BAB06622.
GeneID893083.
KEGGbha:BH2903.
PATRIC18943038. VBIBacHal18977_3020.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000220641.
KOK01182.
OMAVGWNSLY.
OrthoDBEOG6RVFV2.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-2999-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 nameO16G_BACHD
AccessionPrimary (citable) accession number: Q9K8U9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 87 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