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Q9R9H8 (BBMA2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 51. 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:
Intracellular maltogenic amylase

EC=3.2.1.-
Gene names
Name:bbmA
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-(1,3)-glycosidic linkages upon the hydrolysis of substrate at concentrations of 5% or higher. Ref.1

Subunit structure

Monomer or homodimer; in equilibrium. Ref.1

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. BbmA subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Stable at pH 6.0 and about 80% of the enzyme activity remained between pH 7.0 and pH 8.0. Ref.1

Temperature dependence:

Optimum temperature is 40-45 degrees Celsius.

Sequence caution

The sequence AAF23874.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

hydrolase activity, hydrolyzing O-glycosyl compounds

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Intracellular maltogenic amylase
PRO_0000366978

Sites

Active site3271Nucleophile By similarity
Active site3561Proton donor By similarity
Site4231Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R9H8 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 00EE31A2A54BE14F

FASTA58868,700
        10         20         30         40         50         60 
MEYAAIHHQP FSTDAYSYDG RTVHIKIRTK KGDADHIRFI WGDPYEYNDG KWSANEQPMR 

        70         80         90        100        110        120 
KIAATEMHDY WFAEVVPPFR RLQYAFVVTD DHEDIFFGSS GVCPYNEKTL ETIHYYFKFP 

       130        140        150        160        170        180 
FVHEADTFQA PEWVKSTVWY QIFPERFANG REDLSPKNAL PWGSKDPGVN DFFGGDLQGI 

       190        200        210        220        230        240 
VDKLDYLEDL GVNGIYLTPI FSAPSNHKYD TLDYFSIDPH FGDPEIFRTL VSQLHQRGMR 

       250        260        270        280        290        300 
IMLDAVFNHI GSASPQWQDV VKNGDQSRYK DWFHIHSFPV TDDNYDRFAF TADMPKLNTA 

       310        320        330        340        350        360 
NPEVQKYLLD IALYWIREFD IDGWRLDVAN EVDHVFWKTF RQAVSTEKPD VYILGEIWHS 

       370        380        390        400        410        420 
AEPWLRGDEF HAAMNYPFTE PMIEYFADQT ISASRMAHRV NAHLMNGMKQ ANEVMFNLLD 

       430        440        450        460        470        480 
SHDTKRLLTR CRNDEKKARA LLAFMFAQTG SPCIYYGTEI GLDGENDPLC RKCMVWEKEK 

       490        500        510        520        530        540 
QNQDMLQFMK RLIALRKQEN TLLTEGHLEW NLLDDKNDFI SFSRTLDEKI LIYFFNQGNV 

       550        560        570        580 
VQHISLRELN IDRNNKICDA WTEQPLHYHD VIAVQPGEFL ILSAAAPV 

« Hide

References

[1]"Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2."
Cho H.-Y., Kim Y.-W., Kim T.-J., Lee H.-S., Kim D.-Y., Kim J.-W., Lee Y.-W., Leed S.-B., Park K.-H.
Biochim. Biophys. Acta 1478:333-340(2000) [PubMed: 10825545] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT.
Strain: SUH4-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF115340 Genomic DNA. Translation: AAF23874.1. Different initiation.

3D structure databases

HSSPHSSP built from PDB template 1J0H based on UniProtKB P38940.
ProteinModelPortalQ9R9H8.
ModBaseSearch...

Protein family/group databases

CAZyCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBBMA2_BACSU
AccessionPrimary (citable) accession number: Q9R9H8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: June 28, 2011
This is version 51 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families