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O06988 (BBMA1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:yvdF
Ordered Locus Names:BSU34620
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subunit structure

Monomer or homodimer; in equilibrium By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. BbmA subfamily.

Sequence caution

The sequence CAB08035.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB15467.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
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_0000366977

Sites

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

Sequences

Sequence LengthMass (Da)Tools
O06988 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 6132681370919DFE

FASTA58868,722
        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 PWGSKDPDVN DFFGGDLQGI 

       190        200        210        220        230        240 
VDKLDYLEDL GVNGIYLTPI FSAPSNHKYD TLDYFSIDPH FGDPELFRTL 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 GLNGENDPLC RKCMVWEKEK 

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

       550        560        570        580 
VQHVSLRELN IDRNKKICDA WTEQPLQHHD VIAVQPGEFL ILSAAAPV

« Hide

References

« Hide 'large scale' references
[1]Denizot F.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z94043 Genomic DNA. Translation: CAB08035.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15467.1. Different initiation.
PIRF70033.
RefSeqNP_391342.1. NC_000964.3.

3D structure databases

HSSPHSSP built from PDB template 1J0H based on UniProtKB P38940.
ProteinModelPortalO06988.
SMRO06988. Positions 1-585.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001469; EBBACP00000001469; EBBACG00000001467.
GeneID936514.
GenomeReviewsGene locus BSU34620 in contig AL009126_GR.
KEGGbsu:BSU34620.
NMPDRfig|224308.1.peg.3468.
PATRIC18978928. VBIBacSub10457_3626.

Organism-specific databases

GenoListBSU34620. [Micado]

Phylogenomic databases

GeneTreeEBGT00070000031973.
HOGENOMHBG726713.
OMAETVWYQI.
PhylomeDBO06988.
ProtClustDBCLSK561347.

Enzyme and pathway databases

BioCycBSUB:BSU34620-MONOMER.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
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:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA: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 nameBBMA1_BACSU
AccessionPrimary (citable) accession number: O06988
Secondary accession number(s): Q795G7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 78 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

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