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Reviewed, UniProtKB/Swiss-Prot P00693 (AMY1_HORVU)

Last modified January 19, 2010. Version 93. 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 A isozyme
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    AMY1
    Low pI alpha-amylase
Gene names
Name: AMY1.1
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 length438 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 By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted › extracellular space.

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.

Mutagenesis experiments indicate that His-117 and His-314 participate in transition state stabilization but not directly in catalysis.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 438414Alpha-amylase type A isozyme
PRO_0000001404

Sites

Active site2041Nucleophile
Active site2291Proton donor
Active site3151
Metal binding1161Calcium 1 By similarity
Metal binding1331Calcium 2 By similarity
Metal binding1361Calcium 2 By similarity
Metal binding1381Calcium 2 By similarity
Metal binding1421Calcium 2 By similarity
Metal binding1521Calcium 3 By similarity
Metal binding1631Calcium 3 By similarity
Metal binding1661Calcium 3; via carbonyl oxygen By similarity
Metal binding1671Calcium 1 By similarity
Metal binding1681Calcium 1; via carbonyl oxygen By similarity
Metal binding1711Calcium 3; via carbonyl oxygen By similarity
Metal binding1731Calcium 1 By similarity
Metal binding1731Calcium 3 By similarity

Experimental info

Mutagenesis1171H → N: 20-fold decrease in activity. Ref.2
Mutagenesis2041D → N: Loss of activity. Ref.2
Mutagenesis2291E → Q: Loss of activity. Ref.2
Mutagenesis3031W → A: 10-fold decrease in affinity for starch granules. Ref.2
Mutagenesis3141H → N: 10-fold decrease in activity. Ref.2
Mutagenesis3151D → N: Loss of activity. Ref.2

Secondary structure

1 ................................................................................. 438
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00693-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2393FDAC51E80F51

FASTA43847,796
        10         20         30         40         50         60 
MGKNGSLCCF SLLLLLLLAG LASGHQVLFQ GFNWESWKQS GGWYNMMMGK VDDIAAAGVT 

        70         80         90        100        110        120 
HVWLPPPSHS VSNEGYMPGR LYDIDASKYG NAAELKSLIG ALHGKGVQAI ADIVINHRCA 

       130        140        150        160        170        180 
DYKDSRGIYC IFEGGTSDGR LDWGPHMICR DDTKYSDGTA NLDTGADFAA APDIDHLNDR 

       190        200        210        220        230        240 
VQRELKEWLL WLKSDLGFDA WRLDFARGYS PEMAKVYIDG TSPSLAVAEV WDNMATGGDG 

       250        260        270        280        290        300 
KPNYDQDAHR QNLVNWVDKV GGAASAGMVF DFTTKGILNA AVEGELWRLI DPQGKAPGVM 

       310        320        330        340        350        360 
GWWPAKAATF VDNHDTGSTQ AMWPFPSDKV MQGYAYILTH PGIPCIFYDH FFNWGFKDQI 

       370        380        390        400        410        420 
AALVAIRKRN GITATSALKI LMHEGDAYVA EIDGKVVVKI GSRYDVGAVI PAGFVTSAHG 

       430 
NDYAVWEKNG AAATLQRS

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References

[1]"Isolation and sequence analysis of a barley alpha-amylase cDNA clone."
Rogers J.C., Milliman C.
J. Biol. Chem. 258:8169-8174(1983) [PubMed: 6190808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Himalaya.
Tissue: Aleurone.
[2]"Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1."
Sogaard M., Kadziola A., Haser R., Svensson B.
J. Biol. Chem. 268:22480-22484(1993) [PubMed: 7901200] [Abstract]
Cited for: MUTAGENESIS OF HIS-117; ASP-204; GLU-229; TRP-303; HIS-314 AND ASP-315.
[3]"The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs."
Robert X., Haser R., Gottschalk T.E., Ratajczak F., Driguez H., Svensson B., Aghajari N.
Structure 11:973-984(2003) [PubMed: 12906828] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-428.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01236 mRNA. Translation: AAA32929.1.
PIRALBH. A00846.
UniGeneHv.68

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HT6X-ray1.50A25-429[»]
1P6WX-ray2.00A25-429[»]
1RP8X-ray2.00A25-429[»]
1RP9X-ray2.00A25-429[»]
1RPKX-ray2.00A25-429[»]
2QPSX-ray2.20A25-429[»]
2QPUX-ray1.70A/B/C25-429[»]
3BSGX-ray1.95A25-438[»]
3BSHX-ray3.00A25-438[»]
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Organism-specific databases

GrameneP00693.

Enzyme and pathway databases

BRENDA3.2.1.1. 283.

Gene expression databases

GenevestigatorP00693.

Family and domain databases

InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR006046. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR017853. Glyco_hydro_catalytic_core.
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 nameAMY1_HORVU
AccessionPrimary (citable) accession number: P00693
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 19, 2010
This is version 93 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