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Reviewed, UniProtKB/Swiss-Prot P04063 (AMY2_HORVU)

Last modified October 13, 2009. Version 85. 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:
    Alpha-amylase type B isozyme
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    AMY2-2
    High pI alpha-amylase
Gene names
Name: AMY1.2
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 length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 3 calcium ions per subunit.

Subunit structure

Monomer.

Developmental stage

Production of alpha-amylase is hormonally regulated. Germinating embryos produce the hormone gibberellic acid, which within 10 hours stimulates the aleurone cells covering the endosperm of the seed to produce alpha-amylase. The enzyme then degrades the starch within the endosperm for use by the developing plant embryo.

Induction

Type B isozyme mRNA is undetectable in unstimulated cells and increases a hundred-fold after stimulation with gibberellic acid.

Miscellaneous

There are at least 4 types of alpha-amylase in barley.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Germination
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 427403Alpha-amylase type B isozyme
PRO_0000001405

Sites

Active site2031Nucleophile
Active site2281Proton donor
Active site3131
Metal binding1151Calcium 1
Metal binding1321Calcium 2
Metal binding1351Calcium 2
Metal binding1371Calcium 2
Metal binding1411Calcium 2
Metal binding1511Calcium 3
Metal binding1621Calcium 3
Metal binding1651Calcium 3; via carbonyl oxygen
Metal binding1661Calcium 1
Metal binding1671Calcium 1; via carbonyl oxygen
Metal binding1701Calcium 3; via carbonyl oxygen
Metal binding1721Calcium 1
Metal binding1721Calcium 3

Experimental info

Sequence conflict1341G → D in CAA33298. Ref.1
Sequence conflict195 – 1973IGF → HRL Ref.2
Sequence conflict4251E → Q in CAA33298. Ref.1

Secondary structure

1 ................................................................................ 427
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P04063-1 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: 957C0B16621BF748

FASTA42747,356
        10         20         30         40         50         60 
MANKHLSLSL FLVLLGLSAS LASGQVLFQG FNWESWKHNG GWYNFLMGKV DDIAAAGITH 

        70         80         90        100        110        120 
VWLPPASQSV AEQGYMPGRL YDLDASKYGN KAQLKSLIGA LHGKGVKAIA DIVINHRTAE 

       130        140        150        160        170        180 
HKDGRGIYCI FEGGTPDARL DWGPHMICRD DRPYADGTGN PDTGADFGAA PDIDHLNLRV 

       190        200        210        220        230        240 
QKELVEWLNW LKADIGFDGW RFDFAKGYSA DVAKIYIDRS EPSFAVAEIW TSLAYGGDGK 

       250        260        270        280        290        300 
PNLNQDQHRQ ELVNWVDKVG GKGPATTFDF TTKGILNVAV EGELWRLRGT DGKAPGMIGW 

       310        320        330        340        350        360 
WPAKAVTFVD NHDTGSTQHM WPFPSDRVMQ GYAYILTHPG TPCIFYDHFF DWGLKEEIDR 

       370        380        390        400        410        420 
LVSVRTRHGI HNESKLQIIE ADADLYLAEI DGKVIVKLGP RYDVGNLIPG GFKVAAHGND 


YAVWEKI

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References

[1]"Nucleotide and predicted amino acid sequences of two different genes for high-pI alpha-amylases from barley."
Rahmatullah R.J., Huang J.K., Clark K.L., Reeck G.R., Chandra G.R., Muthukrishnan S.
Plant Mol. Biol. 12:119-121(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Two barley alpha-amylase gene families are regulated differently in aleurone cells."
Rogers J.C.
J. Biol. Chem. 260:3731-3738(1985) [PubMed: 3871776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Crystal and molecular structure of barley alpha-amylase."
Kadziola A., Abe J.-I., Svensson B., Haser R.
J. Mol. Biol. 239:104-121(1994) [PubMed: 8196040] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]"Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9-A resolution."
Vallee F., Kadziola A., Bourne Y., Juy M., Rodenburg K.W., Svensson B., Haser R.
Structure 6:649-659(1998) [PubMed: 9634702] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH BASI.
Strain: cv. Menuet.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X15226 Genomic DNA. Translation: CAA33298.1.
K02637 Genomic DNA. Translation: AAA98790.1.
PIRALBHB. A31960.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AMYX-ray2.80A25-427[»]
1AVAX-ray1.90A/B25-427[»]
1BG9X-ray2.80A25-427[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6097N.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Organism-specific databases

GrameneP04063.

Enzyme and pathway databases

BRENDA3.2.1.1. 283.

Gene expression databases

GenevestigatorP04063.

Family and domain databases

InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR006046. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMY2_HORVU
AccessionPrimary (citable) accession number: P04063
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 15, 1998
Last modified: October 13, 2009
This is version 85 of the entry and version 3 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