Skip Header

Contribute Send feedback
Read comments (?) or add your own

P04750 (AMY6_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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
Clones GRAMY56 and 963
Gene names
Name:AMY1.6
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 length429 AA.
Sequence statusComplete.
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

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 – 429405Alpha-amylase type B isozyme
PRO_0000001407

Regions

Region75 – 762Substrate binding By similarity
Region203 – 2086Substrate binding By similarity
Region301 – 3033Substrate binding By similarity
Region404 – 4063Substrate binding By similarity

Sites

Active site2051Nucleophile By similarity
Active site2301Proton donor By similarity
Metal binding1151Calcium 1 By similarity
Metal binding1321Calcium 2 By similarity
Metal binding1351Calcium 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 binding1671Calcium 1; via carbonyl oxygen By similarity
Metal binding1681Calcium 3 By similarity
Metal binding1691Calcium 3; via carbonyl oxygen By similarity
Metal binding1721Calcium 3; via carbonyl oxygen By similarity
Metal binding1741Calcium 1 By similarity
Metal binding1741Calcium 3 By similarity
Metal binding2091Calcium 1; via carbonyl oxygen By similarity
Binding site2321Substrate By similarity
Binding site2341Substrate By similarity
Binding site2521Substrate By similarity
Binding site2951Substrate By similarity
Binding site3141Substrate By similarity
Binding site3201Substrate By similarity
Binding site3991Substrate By similarity
Binding site4261Substrate By similarity
Site3151Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P04750 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 1C924CA6319D5262

FASTA42947,937
        10         20         30         40         50         60 
MANKHMSLSL FIVLLGLSCS LASGQVLFQG FNWESWKHNG GWYNFLMGKV DDIAAAGVTH 

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

       130        140        150        160        170        180 
RKDGRGIYCI FEGGTPDARL DWGPHMICRD DRPYPDGTGN RPTRTRADFG AAPDIDHLNP 

       190        200        210        220        230        240 
RVQKELVEWL NWLRTDDGFD GWRFDFAKGY SADVAKIYVD RSEPSFAVAE IWTSLAYGGD 

       250        260        270        280        290        300 
GKPNLNQDPH RQELVNWVNK VGGSGPATTF DFTTKGILNV AVEGELWRLR GTDGKAPGMI 

       310        320        330        340        350        360 
GWWPAKAVTF VDNHDTGSTQ HMWPFPSDRV MQGYAYILTH PGNPCIFYDH FFDWGLKEEI 

       370        380        390        400        410        420 
DRLVSIRTRQ GIHSESKLQI MEADADLYLA EIEGKVIVKL GPRYDVGHLI PEGFKVVAHG 


NDYAVWEKV

« Hide

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] (CLONE GRAMY56).
[2]"Expression and regulation of alpha-amylase gene family in barley aleurones."
Huang J.-K., Swegle M., Dandekar A.M., Muthukrishnan S.
J. Mol. Appl. Genet. 2:579-588(1984) [PubMed: 6335720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 380-429 (CLONE 963).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X15227 Genomic DNA. Translation: CAA33299.1.
K02636 mRNA. Translation: AAA32932.1.
PIRJE0406.
UniGeneHv.8295.

3D structure databases

ProteinModelPortalP04750.
SMRP04750. Positions 25-429.
ModBaseSearch...

Protein-protein interaction databases

IntActP04750. 1 interaction.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP04750.

Gene expression databases

GenevestigatorP04750.

Family and domain databases

InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
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:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 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...

Entry information

Entry nameAMY6_HORVU
AccessionPrimary (citable) accession number: P04750
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 90 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents