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P17859 (AMYA_VIGMU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 83. 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
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY1.1
OrganismVigna mungo (Black gram) (Phaseolus mungo)
Taxonomic identifier3915 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna

Protein attributes

Sequence length421 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.

Miscellaneous

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
   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 – 2323 Probable
Chain24 – 421398Alpha-amylase
PRO_0000001417

Regions

Region73 – 742Substrate binding By similarity
Region199 – 2046Substrate binding By similarity
Region295 – 2973Substrate binding By similarity
Region398 – 4003Substrate binding By similarity

Sites

Active site2011Nucleophile By similarity
Active site2261Proton donor By similarity
Metal binding1131Calcium 1 By similarity
Metal binding1301Calcium 2 By similarity
Metal binding1331Calcium 2; via carbonyl oxygen By similarity
Metal binding1351Calcium 2; via carbonyl oxygen By similarity
Metal binding1391Calcium 2 By similarity
Metal binding1491Calcium 3 By similarity
Metal binding1601Calcium 1 By similarity
Metal binding1681Calcium 3; via carbonyl oxygen By similarity
Metal binding1701Calcium 1 By similarity
Metal binding1701Calcium 3 By similarity
Metal binding2051Calcium 1; via carbonyl oxygen By similarity
Binding site2281Substrate By similarity
Binding site2301Substrate By similarity
Binding site2551Substrate By similarity
Binding site2891Substrate By similarity
Binding site3081Substrate By similarity
Binding site3141Substrate By similarity
Binding site3931Substrate By similarity
Binding site4201Substrate By similarity
Site3091Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P17859 [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

« Hide

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].
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalP17859.
SMRP17859. Positions 25-421.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 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: December 14, 2011
This is version 83 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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