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Reviewed, UniProtKB/Swiss-Prot P17859 (AMYA_VIGMU)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
Gene names
Name: AMY1.1
OrganismVigna mungo (Rice bean) (Black gram)
Taxonomic identifier3915 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna

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Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   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: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Probable
Chain24 – 421398Alpha-amylase
PRO_0000001417

Sites

Active site2011Nucleophile By similarity
Active site2261Proton donor By similarity
Active site3091 By similarity
Metal binding1131Calcium 1 By similarity
Metal binding1301Calcium 2 By similarity
Metal binding1331Calcium 2 By similarity
Metal binding1351Calcium 2 By similarity
Metal binding1391Calcium 2 By similarity
Metal binding1491Calcium 3 By similarity
Metal binding1601Calcium 3 By similarity
Metal binding1681Calcium 3; via carbonyl oxygen By similarity
Metal binding1701Calcium 1 By similarity
Metal binding1701Calcium 3 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P17859-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 15CA0DABA3DB4656

FASTA42146,889
        10         20         30         40         50         60 
MDSFSRLSIF CLFISLLPLF SSPALLFQGF NWESSKKGGW YNSLKNSIPD LANAGITHVW 

        70         80         90        100        110        120 
LPPPSQSVSP EGYLPGRLYD LDASKYGSKN ELKSLIAAFH EKGIKCLADI VINHRTAERK 

       130        140        150        160        170        180 
DGRGIYCIFE GGTPDSRQDW GPSFICRDDT AYSDGTGNND SGEGYDAAPD IDHLNPQVQR 

       190        200        210        220        230        240 
ELSEWMNWLK TEIGFDGWRF DFVKGYAPSI SKIYMEQTKP DFAVGEKWDS ISYGQDGKPN 

       250        260        270        280        290        300 
YNQDSHRGAL VNWVESAGGA ITAFDFTTKG ILQAAVQGEL WRLIDPNGKP PGMIGVKPEN 

       310        320        330        340        350        360 
AVTFIDNHDT GSTQRLWPFP SDKVMQGYAY ILTHPGTPSI FYDHFFDWGL KEQIAKLSSI 

       370        380        390        400        410        420 
RLRNGINEKS TVKIMASEGD LYVAKIDNKI MVKIGPKMDL GNLIPSNLHV ATSGQDYAVW 


E

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References

[1]"Nucleotide sequence of cDNA for alpha-amylase from cotyledons of germinating Vigna mungo seeds."
Yamauchi D., Minamikawa T.
Nucleic Acids Res. 18:4250-4250(1990) [PubMed: 2377468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cotyledon.
[2]"Nucleotide sequence of the alpha-amylase gene from Vigna mungo."
Takeuchi H., Yamauchi D., Wada S., Minamikawa T.
Plant Physiol. 103:1459-1459(1993) [PubMed: 8290640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

X53049 mRNA. Translation: CAA37217.1.
X73301 Genomic DNA. Translation: CAA51734.1.
PIRS10514.

3D structure databases

HSSPHSSP built from PDB template 1AVA based on UniProtKB P04063.
SMRP17859. Positions 25-421.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA3.2.1.1. 142156.

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 nameAMYA_VIGMU
AccessionPrimary (citable) accession number: P17859
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 69 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

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