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P06547 (AMYB_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 76. 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:
Beta-amylase

EC=3.2.1.2
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-amylase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636
Chain37 – 575539Beta-amylase
PRO_0000001454

Regions

Region396 – 3972Substrate binding By similarity

Sites

Active site1991Proton donor By similarity
Active site3951Proton acceptor By similarity
Binding site771Substrate By similarity
Binding site1171Substrate By similarity
Binding site1251Substrate By similarity
Binding site3151Substrate By similarity
Binding site3201Substrate By similarity
Binding site3581Substrate By similarity
Binding site4241Substrate By similarity

Amino acid modifications

Disulfide bond119 ↔ 127 By similarity

Sequences

Sequence LengthMass (Da)Tools
P06547 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 724E8C0D66B4A258

FASTA57562,899
        10         20         30         40         50         60 
MLHSQKRIWK KIGLCLLSFI LGITVFTGSF GSKAEAAVAG DFQVSVMGPL AKVTDWNSFK 

        70         80         90        100        110        120 
NQLTTLKNNG VYAITTDVWW GYVESAGDNQ FDWSYYKTYA DTVKQAGLKW VPIISTHRCG 

       130        140        150        160        170        180 
GNVGDDCNIP LPSWLWSKGS ADEMQFKDES GYVNNESLSP FWSGVGKQYD ELYASFAQNF 

       190        200        210        220        230        240 
SAYKDMIPKI YLSGGPSGEL RYPSYYPAAG WSYPARGKFQ VYTETAKSAF RTAMTTKYGS 

       250        260        270        280        290        300 
LDKINAAWGT NLTSMSQISP PTDSDGFYTG GGYNITYGKD FLSWYQSVLE NHLGVIGAAA 

       310        320        330        340        350        360 
HKNFDPVFGV RIGAKISGIH WQMNNPSMPH SAEHAGGYYD YNRLIQKFKD TDLDLTFTAL 

       370        380        390        400        410        420 
EMYDSGTAPN YSLPSTLVDT VSSIANSKGV RLNGENALPT GGSGFQKIEE KITRFGYNGF 

       430        440        450        460        470        480 
TLLRINNIVN SDGSPTAEMS SFKNYVIKHA KPAGDGGGNP VNSVTIYYKK GFNSPYIHYR 

       490        500        510        520        530        540 
PAGGTWTDVP GVKMPDSEIS GYAKITLDIG SASQLEAAFN DGNNQWDSNN MRNYFFSPGT 

       550        560        570 
STYIPGTNGT AGSIQAGPPI TSSDFQALPA YEMSI 

« Hide

References

[1]"Molecular cloning and characterization of the beta-amylase gene from Bacillus circulans."
Siggens K.W.
Mol. Microbiol. 1:86-91(1987) [PubMed: 2455212] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCIB 11033.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00523 Genomic DNA. Translation: CAA68578.1.
PIRS03745.

3D structure databases

ProteinModelPortalP06547.
ModBaseSearch...

Protein family/group databases

CAZyCBM25. Carbohydrate-Binding Module Family 25.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005085. CBM_fam25.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF03423. CBM_25. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYB_BACCI
AccessionPrimary (citable) accession number: P06547
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: September 21, 2011
This is version 76 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

SIMILARITY comments

Index of protein domains and families