Skip Header

Contribute Send feedback
Read comments (?) or add your own

O06994 (O16G1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. 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
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 1
EC=3.2.1.10
Alternative name(s):
Dextrin 6-alpha-D-glucanohydrolase
Oligosaccharide alpha-1,6-glucosidase 1
Sucrase-isomaltase 1
Short name=Isomaltase 1
Gene names
Name:malL
Synonyms:yvdL
Ordered Locus Names:BSU34560
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

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

General annotation (Comments)

Function

Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.

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:

Optimum temperature is 42 degrees Celsius.

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Oligo-1,6-glucosidase 1
PRO_0000054317

Sites

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

Sequences

Sequence LengthMass (Da)Tools
O06994 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 2B43E9A4AD65A222

FASTA56166,081
        10         20         30         40         50         60 
MSEWWKEAVV YQIYPRSFYD ANGDGFGDLQ GVIQKLDYIK NLGADVIWLS PVFDSPQDDN 

        70         80         90        100        110        120 
GYDISDYKNM YEKFGTNEDM FQLIDEVHKR GMKIVMDLVV NHTSDEHAWF AESRKSKDNP 

       130        140        150        160        170        180 
YRDYYLWKDP KPDGSEPNNW GSIFSGSAWT YDEGTGQYYL HYFSKKQPDL NWENEAVRRE 

       190        200        210        220        230        240 
VYDVMRFWMD RGVDGWRMDV IGSISKYTDF PDYETDHSRS YIVGRYHSNG PRLHEFIQEM 

       250        260        270        280        290        300 
NREVLSHYDC MTVGEANGSD IEEAKKYTDA SRQELNMIFT FEHMDIDKEQ NSPNGKWQIK 

       310        320        330        340        350        360 
PFDLIALKKT MTRWQTGLMN VGWNTLYFEN HDQPRVISRW GNDRKLRKEC AKAFATVLHG 

       370        380        390        400        410        420 
MKGTPFIYQG EEIGMVNSDM PLEMYDDLEI KNAYRELVVE NKTMSEKEFV KAVMIKGRDH 

       430        440        450        460        470        480 
ARTPMQWDAG KHAGFTAGDP WIPVNSRYQD INVKESLEDQ DSIFFYYQKL IQLRKQYKIM 

       490        500        510        520        530        540 
IYGDYQLLQE NDPQVFSYLR EYRGEKLLVV VNLSEEKALF EAPPELIHER WKVLISNYPQ 

       550        560 
ERADLKSISL KPYEAVMGIS I

« Hide

References

« Hide 'large scale' references
[1]Denizot F.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
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]"Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis."
Schoenert S., Buder T., Dahl M.K.
J. Bacteriol. 180:2574-2578(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization."
Schoenert S., Buder T., Dahl M.K.
Res. Microbiol. 150:167-177(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z94043 Genomic DNA. Translation: CAB08041.1.
AL009126 Genomic DNA. Translation: CAB15461.1.
PIRD70034.
RefSeqNP_391336.1. NC_000964.3.

3D structure databases

ProteinModelPortalO06994.
SMRO06994. Positions 2-559.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU34560.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbO06994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15461; CAB15461; BSU34560.
GeneID938623.
KEGGbsu:BSU34560.
PATRIC18978916. VBIBacSub10457_3620.

Organism-specific databases

GenoListBSU34560. [Micado]

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000220641.
KOK01182.
OMAIRTNGAT.
ProtClustDBCLSK237159.

Enzyme and pathway databases

BioCycBSUB:BSU34560-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. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameO16G1_BACSU
AccessionPrimary (citable) accession number: O06994
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents