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Reviewed, UniProtKB/Swiss-Prot P16098 (AMYB_HORVU)

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: BMY1
Synonyms: AMYB
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

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Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainRepeat
   Molecular functionGlycosidase
Hydrolase
   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

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535Beta-amylase
PRO_0000153933

Regions

Repeat489 – 499111
Repeat500 – 510112
Repeat511 – 521113
Repeat522 – 532114; approximate
Region489 – 532444 X 11 AA tandem repeats

Sites

Active site1841 By similarity
Active site3781 By similarity

Experimental info

Sequence conflict2331V → A Ref.2
Sequence conflict2331V → A Ref.3
Sequence conflict3471L → S Ref.2
Sequence conflict3471L → S Ref.3
Sequence conflict5271I → M Ref.2
Sequence conflict5271I → M Ref.3

Secondary structure

1 ................................................................................... 535
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P16098-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: FFDA4CED53E9A89E

FASTA53559,647
        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 ENMKDFLDAG VIVDIEVGLG 

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

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

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

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

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

       490        500        510        520        530 
QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGIGGE LPATM

« Hide

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References

[1]"Primary structure and differential expression of beta-amylase in normal and mutant barleys."
Kreis M., Williamson M., Buxton B., Pywell J., Hejgaard J., Svendsen I.
Eur. J. Biochem. 169:517-525(1987) [PubMed: 2446870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE.
Tissue: Endosperm.
[2]"A structural gene encoding beta-amylase of barley."
Yoshigi N., Okada Y., Sahara H., Tamaki T.
Biosci. Biotechnol. Biochem. 59:1991-1993(1995) [PubMed: 8534999] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Haruna Two-rows.
[3]"PCR cloning and sequencing of the beta-amylase cDNA from barley."
Yoshigi N., Okada Y., Sahara H., Koshino S.
J. Biochem. 115:47-51(1994) [PubMed: 8188635] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Haruna Two-rows.
[4]"The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution."
Mikami B., Yoon H.-J., Yoshigi N.
J. Mol. Biol. 285:1235-1243(1999) [PubMed: 9918723] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-504.

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Cross-references

Sequence databases

X52321 mRNA. Translation: CAA36556.1.
D49999 Genomic DNA. Translation: BAA08741.1.
D21349 mRNA. Translation: BAA04815.1.
PIRS00222.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B1YX-ray2.50A6-504[»]
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Organism-specific databases

GrameneP16098.

Enzyme and pathway databases

BRENDA3.2.1.2. 283.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYB_HORVU
AccessionPrimary (citable) accession number: P16098
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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