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Q8VZ56

- AMY1_ARATH

UniProt

Q8VZ56 - AMY1_ARATH

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Protein

Alpha-amylase 1

Gene
AMY1, At4g25000, F13M23.140
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Possesses alpha-amylase activity in vitro, but seems not required for breakdown of transitory starch in leaves.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactori

Binds 3 calcium ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161Calcium 1 By similarity
Metal bindingi133 – 1331Calcium 2 By similarity
Metal bindingi136 – 1361Calcium 2; via carbonyl oxygen By similarity
Metal bindingi138 – 1381Calcium 2; via carbonyl oxygen By similarity
Metal bindingi142 – 1421Calcium 2 By similarity
Metal bindingi152 – 1521Calcium 3 By similarity
Metal bindingi162 – 1621Calcium 1 By similarity
Metal bindingi165 – 1651Calcium 1; via carbonyl oxygen By similarity
Metal bindingi166 – 1661Calcium 3 By similarity
Metal bindingi167 – 1671Calcium 3; via carbonyl oxygen By similarity
Metal bindingi170 – 1701Calcium 3; via carbonyl oxygen By similarity
Metal bindingi172 – 1721Calcium 1 By similarity
Metal bindingi172 – 1721Calcium 3 By similarity
Active sitei203 – 2031Nucleophile By similarity
Metal bindingi207 – 2071Calcium 1; via carbonyl oxygen By similarity
Active sitei228 – 2281Proton donor By similarity
Binding sitei230 – 2301Substrate By similarity
Binding sitei292 – 2921Substrate By similarity
Binding sitei311 – 3111Substrate By similarity
Sitei312 – 3121Transition state stabilizer By similarity
Binding sitei393 – 3931Substrate By similarity
Binding sitei420 – 4201Substrate By similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: TAIR
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. response to abscisic acid Source: TAIR
  3. response to gibberellin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G25000-MONOMER.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase 1 (EC:3.2.1.1)
Short name:
AtAMY1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:AMY1
Ordered Locus Names:At4g25000
ORF Names:F13M23.140
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G25000.

Subcellular locationi

Secretedextracellular spaceapoplast Inferred 1 Publication

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. extracellular region Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

Pathology & Biotechi

Disruption phenotypei

Early flowering.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Chaini25 – 423399Alpha-amylase 1PRO_0000418861Add
BLAST

Proteomic databases

PRIDEiQ8VZ56.

Expressioni

Tissue specificityi

Expressed in leaves, stems, flowers and developing siliques.1 Publication

Developmental stagei

Up-regulated during leaf senescence.

Inductioni

By gibberellin, abscisic acid (ABA), heat shock and infection with the bacterial pathogen P.syringae. Not regulated by transition from dark to light.3 Publications

Gene expression databases

GenevestigatoriQ8VZ56.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

STRINGi3702.AT4G25000.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8VZ56.
SMRiQ8VZ56. Positions 27-422.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 772Substrate binding By similarity
Regioni201 – 2066Substrate binding By similarity
Regioni298 – 3003Substrate binding By similarity
Regioni398 – 4003Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ8VZ56.
KOiK01176.
OMAiYRDYEEW.
PhylomeDBiQ8VZ56.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR012850. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFiPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VZ56-1 [UniParc]FASTAAdd to Basket

« Hide

MTSLHTLLFS SLLFFIVFPT FTFSSTLLFQ SFNWESWKKE GGFYNSLHNS    50
IDDIANAGIT HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK 100
ALNQKGIKAL ADIVINHRTA ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR 150
NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV QKELSEWMNW LKTEIGFHGW 200
RFDYVRGYAS SITKLYVQNT SPDFAVGEKW DDMKYGGDGK LDYDQNEHRS 250
GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGMIGIM 300
PGNAVTFIDN HDTFRTWVFP SDKVLLGYVY ILTHPGTPCI FYNHYIEWGL 350
KESISKLVAI RNKNGIGSTS SVTIKAAEAD LYLAMIDDKV IMKIGPKQDV 400
GTLVPSNFAL AYSGLDFAVW EKK 423
Length:423
Mass (Da):47,378
Last modified:March 1, 2002 - v1
Checksum:i10D2119B6EA572EC
GO

Sequence cautioni

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191V → I in AAM64582. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT05521.
RefSeqiNP_567714.1. NM_118632.2.
UniGeneiAt.28556.

Genome annotation databases

EnsemblPlantsiAT4G25000.1; AT4G25000.1; AT4G25000.
GeneIDi828603.
KEGGiath:AT4G25000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T05521.
RefSeqi NP_567714.1. NM_118632.2.
UniGenei At.28556.

3D structure databases

ProteinModelPortali Q8VZ56.
SMRi Q8VZ56. Positions 27-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G25000.1-P.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEi Q8VZ56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G25000.1 ; AT4G25000.1 ; AT4G25000 .
GeneIDi 828603.
KEGGi ath:AT4G25000.

Organism-specific databases

TAIRi AT4G25000.

Phylogenomic databases

InParanoidi Q8VZ56.
KOi K01176.
OMAi YRDYEEW.
PhylomeDBi Q8VZ56.

Enzyme and pathway databases

BioCyci ARA:AT4G25000-MONOMER.

Gene expression databases

Genevestigatori Q8VZ56.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR012850. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001028. Alph-amls_plant. 1 hit.
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00810. Alpha-amyl_C2. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiAMY1_ARATH
AccessioniPrimary (citable) accession number: Q8VZ56
Secondary accession number(s): Q8LBS5, Q9SW26
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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