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O65015 (AMYB_TRIRP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BMY1
OrganismTrifolium repens (Creeping white clover)
Taxonomic identifier3899 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Trifolium

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
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

Chain1 – 496496Beta-amylase
PRO_0000153939

Regions

Region382 – 3832Substrate binding By similarity

Sites

Active site1871Proton donor By similarity
Active site3811Proton acceptor By similarity
Binding site541Substrate By similarity
Binding site941Substrate By similarity
Binding site1021Substrate By similarity
Binding site2961Substrate By similarity
Binding site3011Substrate By similarity
Binding site3431Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O65015 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8FC446AB7C927F19

FASTA49656,088
        10         20         30         40         50         60 
MATSNKNMLL NYVPVYVMLP LGVINVNNVF EDPDGLKEQL VQLRAAGVDG VMVDVWWGII 

        70         80         90        100        110        120 
EQKGPKEYDW SAYKSLFQLV QECGLKLQAI MSFHQCGGNV GDVVTIPIPQ WVLDIGESDP 

       130        140        150        160        170        180 
DIFYTNRSGT RDKEYLTVGV DNKPIFHGRT AIEIYSDYMK SFRENMSEFL KSELIIDIEV 

       190        200        210        220        230        240 
GLGPAGELRY PSYPQNQGWV FPGIGEFQCY DKYLKADFKA AAAKAGHSEW ELPDDAGTYN 

       250        260        270        280        290        300 
DIPESTEFFK TNGTYLTEKG KFFLTWYSNQ LLNHGDQILD EANKAFLGCK VKLAIKVSGI 

       310        320        330        340        350        360 
HWWYKAQNHA AELTAGYYNL DDRDGYRPIA KMVSRHHGIL NFTCLEMRDS EQSSDAQSAP 

       370        380        390        400        410        420 
QELVQQVLSG GWRENIEVAG ENALSRYDAT AYNQIILNAR PQGVNKDGPP KLRMYGVTYL 

       430        440        450        460        470        480 
RLSDDLLQES NFEIFKKFVV KMHADQSHCD DPQEYNHAIP PLKRSGPNIP VDDLLEATKP 

       490 
ILPFPWDSET DMKVDG

« Hide

References

[1]"Nucleotide sequence of a beta-amylase cDNA from white clover stollons."
Gallagher J., Gana J.A., Pollock C., Cunningham S.M., Volenec J.J.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF049098 mRNA. Translation: AAD04259.1.
PIRT08117.

3D structure databases

ProteinModelPortalO65015.
SMRO65015. Positions 7-496.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
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_TRIRP
AccessionPrimary (citable) accession number: O65015
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: May 31, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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