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Reviewed, UniProtKB/Swiss-Prot P36924 (AMYB_BACCE)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-amylase
    EC=3.2.1.2
Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
Gene names
Name: spoII
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – 546516Beta-amylase
PRO_0000001453

Regions

Domain444 – 546103CBM20

Sites

Active site2021
Active site3971
Metal binding861Calcium
Metal binding901Calcium
Metal binding911Calcium
Metal binding1711Calcium
Metal binding1741Calcium

Amino acid modifications

Disulfide bond121 ↔ 129

Secondary structure

1 ............................................................................................. 546
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P36924-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: A8F7CFC96ED6979B

FASTA54661,629
        10         20         30         40         50         60 
MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET 

        70         80         90        100        110        120 
FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ 

       130        140        150        160        170        180 
CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA 

       190        200        210        220        230        240 
AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK 

       250        260        270        280        290        300 
YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE 

       310        320        330        340        350        360 
LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT 

       370        380        390        400        410        420 
CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF 

       430        440        450        460        470        480 
AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD 

       490        500        510        520        530        540 
TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT 


SHTSSW

« Hide

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References

[1]"Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme."
Nanmori T., Nagai M., Shimizu Y., Shinke R., Mikami B.
Appl. Environ. Microbiol. 59:623-627(1993) [PubMed: 8434930] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: BQ10-S1.
[2]Nanmori T., Mikami B., Shimizu Y.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose."
Mikami B., Adachi M., Kage T., Sarikaya E., Nanmori T., Shinke R., Utsumi S.
Biochemistry 38:7050-7061(1999) [PubMed: 10353816] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB024519 Genomic DNA. Translation: BAA75890.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B90X-ray2.50A31-546[»]
1B9ZX-ray2.10A31-546[»]
1CQYX-ray1.95A448-546[»]
1ITCX-ray2.10A31-546[»]
1J0YX-ray2.10A/B/C/D31-546[»]
1J0ZX-ray2.20A/B/C/D31-546[»]
1J10X-ray2.10A/B/C/D31-546[»]
1J11X-ray2.00A/B/C/D31-546[»]
1J12X-ray2.10A/B/C/D31-546[»]
1J18X-ray2.00A31-546[»]
1VEMX-ray1.85A31-546[»]
1VENX-ray2.02A31-546[»]
1VEOX-ray2.12A31-546[»]
1VEPX-ray2.06A31-546[»]
5BCAX-ray2.20A/B/C/D31-546[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Enzyme and pathway databases

BRENDA3.2.1.2. 604.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR002044. Glyco_hydro_carb-bd.
IPR013781. Glyco_hydro_sg_catalytic.
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.
PfamPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
ProDomPD001568. Glyco_hydro_CBD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYB_BACCE
AccessionPrimary (citable) accession number: P36924
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 11, 2002
Last modified: June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents