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P16098 (AMYB_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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:BMY1
Synonyms:AMYB
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
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.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-7799617,EBI-7799617

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
Region379 – 3802Substrate binding By similarity
Region489 – 532444 X 11 AA tandem repeats

Sites

Active site1841Proton donor By similarity
Active site3781Proton acceptor By similarity
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

Experimental info

Sequence conflict2331V → A in BAA08741. Ref.2
Sequence conflict2331V → A in BAA04815. Ref.3
Sequence conflict3471L → S in BAA08741. Ref.2
Sequence conflict3471L → S in BAA04815. Ref.3
Sequence conflict5271I → M in BAA08741. Ref.2
Sequence conflict5271I → M in BAA04815. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P16098 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-504.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52321 mRNA. Translation: CAA36556.1.
D49999 Genomic DNA. Translation: BAA08741.1.
D21349 mRNA. Translation: BAA04815.1.
PIRS00222.
UniGeneHv.2064.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1YX-ray2.50A6-504[»]
2XFFX-ray1.31A1-535[»]
2XFRX-ray0.97A1-535[»]
2XFYX-ray1.21A1-535[»]
2XG9X-ray1.80A1-535[»]
2XGBX-ray1.20A1-535[»]
2XGIX-ray1.30A1-535[»]
ProteinModelPortalP16098.
SMRP16098. Positions 5-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-8307128.

Chemistry

BindingDBP16098.
ChEMBLCHEMBL4371.

Protein family/group databases

Allergome420. Hor v 17.
CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP16098.

Gene expression databases

GenevestigatorP16098.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16098.

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: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries