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P04063 (AMY2_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

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.

Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Region75 – 762Substrate binding By similarity
Region201 – 2066Substrate binding
Region299 – 3013Substrate binding
Region402 – 4043Substrate binding By similarity

Sites

Active site2031Nucleophile Ref.4
Active site2281Proton donor Ref.4
Metal binding1151Calcium 1
Metal binding1321Calcium 2
Metal binding1351Calcium 2; via carbonyl oxygen
Metal binding1371Calcium 2; via carbonyl oxygen
Metal binding1411Calcium 2
Metal binding1511Calcium 3
Metal binding1621Calcium 1
Metal binding1651Calcium 1; via carbonyl oxygen
Metal binding1661Calcium 3
Metal binding1671Calcium 3; via carbonyl oxygen
Metal binding1701Calcium 3; via carbonyl oxygen
Metal binding1721Calcium 1
Metal binding1721Calcium 3
Metal binding2071Calcium 1; via carbonyl oxygen
Binding site2301Substrate
Binding site2321Substrate
Binding site2501Substrate
Binding site2571Substrate
Binding site2931Substrate By similarity
Binding site3121Substrate
Binding site3181Substrate By similarity
Binding site3971Substrate By similarity
Binding site4241Substrate By similarity
Site3131Transition state stabilizer

Experimental info

Sequence conflict1341G → D in CAA33298. Ref.1
Sequence conflict4251E → Q in CAA33298. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04063 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS.
[4]"Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis."
Kadziola A., Sogaard M., Svensson B., Haser R.
J. Mol. Biol. 278:205-217(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-427 IN COMPLEX WITH CALCIUM IONS AND ACARBOSE, ACTIVE SITE.
[5]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH BASI AND CALCIUM IONS.
Strain: cv. Menuet.

Cross-references

Sequence databases

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

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMYX-ray2.80A25-427[»]
1AVAX-ray1.90A/B25-427[»]
1BG9X-ray2.80A25-427[»]
ProteinModelPortalP04063.
SMRP04063. Positions 25-427.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6097N.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP04063.

Enzyme and pathway databases

BRENDA3.2.1.1. 2687.

Gene expression databases

GenevestigatorP04063.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 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]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04063.

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: April 3, 2013
This is version 106 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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