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P82993 (AMYB_HORVS) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 40. 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
Beta-Amy1
Gene names
Name:BMY1
OrganismHordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum)
Taxonomic identifier77009 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the liberation of maltose from 1,4-alpha-D glucans. Ref.1 Ref.2

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 By similarity. UniProtKB P10538

Tissue specificity

Endosperm. Ref.2

Polymorphism

There are at least three alleles; SD2H; SD1 and SD2L. The sequence of SD2H is shown here. Ref.2

Miscellaneous

The three alleles show different thermostabilities and different affinities for soluble starch. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionGlycosidase
Hydrolase
   PTMAcetylation
   Technical termDirect 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

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22Removed in mature form Ref.2
PRO_0000279693
Chain3 – 489487Beta-amylase Ref.2
PRO_0000279694
Propeptide490 – 53546Removed in mature form Ref.2
PRO_0000279695

Regions

Repeat489 – 499111
Repeat500 – 510112
Repeat511 – 521113
Repeat522 – 532114; approximate
Region379 – 3802Substrate binding By similarity
Region489 – 532444 X 11 AA tandem repeats

Sites

Active site1841Proton donor By similarity UniProtKB P10538
Active site3781Proton acceptor By similarity UniProtKB P10538
Binding site511Substrate By similarity
Binding site911Substrate By similarity
Binding site991Substrate By similarity
Binding site2931Substrate By similarity
Binding site2981Substrate By similarity
Binding site3401Substrate By similarity
Binding site4181Substrate By similarity

Amino acid modifications

Modified residue31N-acetylvaline Ref.2

Natural variations

Natural variant1651E → D. Ref.2
Natural variant2541T → S. Ref.2
Natural variant4721K → Q. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P82993 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 0B265EAEEF061C9B

FASTA53559,639
        10         20         30         40         50         60 
MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV DVWWGLVEGK 

        70         80         90        100        110        120 
GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA VNIPIPQWVR DVGTRDPDIF 

       130        140        150        160        170        180 
YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ MYADYMTSFR ENMKEFLDAG VIVDIEVGLG 

       190        200        210        220        230        240 
PAGEMRYPSY PQSHGWSFPG IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDAGQYNDTP 

       250        260        270        280        290        300 
ERTQFFRDNG TYLTEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW 

       310        320        330        340        350        360 
YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDSEQS SQAMSAPEEL 

       370        380        390        400        410        420 
VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG INQSGPPEHK LFGFTYLRLS 

       430        440        450        460        470        480 
NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD PMAPLPRSGP EISIEMILQA AKPKLQPFPF 

       490        500        510        520        530 
QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGMGGE LPATM 

« Hide

References

[1]"Allele-dependent barley grain beta-amylase activity."
Erkkila M.J., Leah R., Ahokas H., Cameron-Mills V.
Plant Physiol. 117:679-685(1998) [PubMed: 9625721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: cv. NPGS PI296897.
Tissue: Endosperm.
[2]"The structural basis for functional differences between allelic forms of barley (Hordeum vulgare) beta-amylase."
Eglinton J.K., Lahnstein J., Shirley N., Evans D.E.
Submitted (MAY-2001) to UniProtKB
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, POLYMORPHISM, ACETYLATION AT VAL-3, VARIANTS ASP-165; SER-254 AND GLN-472.
Strain: cv. CPI77146-33.
Tissue: Seed.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061204 Genomic DNA. Translation: AAC67246.1.

3D structure databases

HSSPHSSP built from PDB template 1B1Y based on UniProtKB P16098.
ProteinModelPortalP82993.
SMRP82993. Positions 5-504.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP82993.

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_HORVS
AccessionPrimary (citable) accession number: P82993
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2001
Last modified: September 21, 2011
This is version 40 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