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P36924 (AMYB_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. 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:
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 › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – 546516Beta-amylase
PRO_0000001453

Regions

Domain444 – 546103CBM20
Region398 – 3992Substrate binding

Sites

Active site2021Proton donor
Active site3971Proton acceptor
Metal binding861Calcium
Metal binding901Calcium
Metal binding911Calcium
Metal binding1711Calcium
Metal binding1741Calcium
Binding site791Substrate
Binding site1191Substrate
Binding site1271Substrate
Binding site3171Substrate
Binding site3221Substrate
Binding site3601Substrate
Binding site4271Substrate

Amino acid modifications

Disulfide bond121 ↔ 129 Ref.5

Experimental info

Mutagenesis1941Y → E: Reduces activity by 60%. Ref.5
Mutagenesis1941Y → F: Reduces activity by 64%. Ref.5
Mutagenesis1941Y → H: Reduces activity by 97%. Ref.5
Mutagenesis1941Y → Q: Reduces activity by 80%. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P36924 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents."
Oyama T., Miyake H., Kusunoki M., Nitta Y.
J. Biochem. 133:467-474(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-546 IN COMPLEXES WITH SUBSTRATE ANALOGS.
[5]"Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type."
Hirata A., Adachi M., Utsumi S., Mikami B.
Biochemistry 43:12523-12531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-546 IN COMPLEX WITH CALCIUM IONS AND MALTOSE, MUTAGENESIS OF TYR-194, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB024519 Genomic DNA. Translation: BAA75890.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP36924.
SMRP36924. Positions 31-546.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36924.

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: April 3, 2013
This is version 91 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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