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Q8VZ56 (AMY1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Alpha-amylase 1

Short name=AtAMY1
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY1
Ordered Locus Names:At4g25000
ORF Names:F13M23.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Possesses alpha-amylase activity in vitro, but seems not required for breakdown of transitory starch in leaves. Ref.8

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.

Subcellular location

Secretedextracellular spaceapoplast Probable Ref.8.

Tissue specificity

Expressed in leaves, stems, flowers and developing siliques. Ref.7

Developmental stage

Up-regulated during leaf senescence.

Induction

By gibberellin, abscisic acid (ABA), heat shock and infection with the bacterial pathogen P.syringae. Not regulated by transition from dark to light. Ref.5 Ref.7 Ref.8

Disruption phenotype

Early flowering. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence caution

The sequence CAB36742.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79409.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 423399Alpha-amylase 1
PRO_0000418861

Regions

Region76 – 772Substrate binding By similarity
Region201 – 2066Substrate binding By similarity
Region298 – 3003Substrate binding By similarity
Region398 – 4003Substrate binding By similarity

Sites

Active site2031Nucleophile By similarity
Active site2281Proton donor By similarity
Metal binding1161Calcium 1 By similarity
Metal binding1331Calcium 2 By similarity
Metal binding1361Calcium 2; via carbonyl oxygen By similarity
Metal binding1381Calcium 2; via carbonyl oxygen By similarity
Metal binding1421Calcium 2 By similarity
Metal binding1521Calcium 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 site2921Substrate By similarity
Binding site3111Substrate By similarity
Binding site3931Substrate By similarity
Binding site4201Substrate By similarity
Site3121Transition state stabilizer By similarity

Experimental info

Sequence conflict4191V → I in AAM64582. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8VZ56 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 10D2119B6EA572EC

FASTA42347,378
        10         20         30         40         50         60 
MTSLHTLLFS SLLFFIVFPT FTFSSTLLFQ SFNWESWKKE GGFYNSLHNS IDDIANAGIT 

        70         80         90        100        110        120 
HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK ALNQKGIKAL ADIVINHRTA 

       130        140        150        160        170        180 
ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV 

       190        200        210        220        230        240 
QKELSEWMNW LKTEIGFHGW RFDYVRGYAS SITKLYVQNT SPDFAVGEKW DDMKYGGDGK 

       250        260        270        280        290        300 
LDYDQNEHRS GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGMIGIM 

       310        320        330        340        350        360 
PGNAVTFIDN HDTFRTWVFP SDKVLLGYVY ILTHPGTPCI FYNHYIEWGL KESISKLVAI 

       370        380        390        400        410        420 
RNKNGIGSTS SVTIKAAEAD LYLAMIDDKV IMKIGPKQDV GTLVPSNFAL AYSGLDFAVW 


EKK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Diurnal changes in the transcriptome encoding enzymes of starch metabolism provide evidence for both transcriptional and posttranscriptional regulation of starch metabolism in Arabidopsis leaves."
Smith S.M., Fulton D.C., Chia T., Thorneycroft D., Chapple A., Dunstan H., Hylton C., Zeeman S.C., Smith A.M.
Plant Physiol. 136:2687-2699(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves."
Yu T.S., Zeeman S.C., Thorneycroft D., Fulton D.C., Dunstan H., Lue W.L., Hegemann B., Tung S.Y., Umemoto T., Chapple A., Tsai D.L., Wang S.M., Smith A.M., Chen J., Smith S.M.
J. Biol. Chem. 280:9773-9779(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Contribution of gibberellins to the formation of Arabidopsis seed coat through starch degradation."
Kim Y.C., Nakajima M., Nakayama A., Yamaguchi I.
Plant Cell Physiol. 46:1317-1325(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]"An alpha-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress."
Doyle E.A., Lane A.M., Sides J.M., Mudgett M.B., Monroe J.D.
Plant Cell Environ. 30:388-398(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL035523 Genomic DNA. Translation: CAB36742.1. Sequence problems.
AL161562 Genomic DNA. Translation: CAB79409.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84990.1.
AY065233 mRNA. Translation: AAL38709.1.
AY117294 mRNA. Translation: AAM51369.1.
AY087021 mRNA. Translation: AAM64582.1.
PIRT05521.
RefSeqNP_567714.1. NM_118632.2.
UniGeneAt.28556.

3D structure databases

ProteinModelPortalQ8VZ56.
SMRQ8VZ56. Positions 27-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G25000.1-P.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEQ8VZ56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G25000.1; AT4G25000.1; AT4G25000.
GeneID828603.
KEGGath:AT4G25000.

Organism-specific databases

TAIRAT4G25000.

Phylogenomic databases

InParanoidQ8VZ56.
KOK01176.
OMAYRDYEEW.
PhylomeDBQ8VZ56.

Enzyme and pathway databases

BioCycARA:AT4G25000-MONOMER.

Gene expression databases

GenevestigatorQ8VZ56.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY1_ARATH
AccessionPrimary (citable) accession number: Q8VZ56
Secondary accession number(s): Q8LBS5, Q9SW26
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names