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P04747 (AMY3_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Clone PHV19
Gene names
Name:AMY1.3
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 length368 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

Monomer By similarity.

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.

Miscellaneous

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

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

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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – ›368›344Alpha-amylase type B isozyme
PRO_0000001406

Regions

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

Sites

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

Experimental info

Non-terminal residue3681

Sequences

Sequence LengthMass (Da)Tools
P04747 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A237EF55793BA93B

FASTA36840,787
        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 FEGVTPDARL DWGPHMICRD DRPYADGTGN PDTGADFGAA PDIDHLNLRV 

       190        200        210        220        230        240 
QKELAEWLNW 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 


LVSVRTGA

« Hide

References

[1]"The effects of gibberellic acid and abscisic acid on alpha-amylase mRNA levels in barley aleurone layers studies using an alpha amylase cDNA clone."
Chandler P.M., Zwar J.A., Jacobsen J.V., Higgins T.J.V., Inglis A.S.
Plant Mol. Biol. 3:407-418(1984) [Agricola: IND85038090]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		K02638 mRNA. Translation: AAA32933.1.

3D structure databases

ProteinModelPortalP04747.
SMRP04747. Positions 25-366.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP04747.

Gene expression databases

GenevestigatorP04747.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY3_HORVU
AccessionPrimary (citable) accession number: P04747
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: December 14, 2011
This is version 88 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

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