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Q8VZ56

- AMY1_ARATH

UniProt

Q8VZ56 - AMY1_ARATH

Protein

Alpha-amylase 1

Gene

AMY1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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 1By similarity
    Metal bindingi133 – 1331Calcium 2By similarity
    Metal bindingi136 – 1361Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi138 – 1381Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi142 – 1421Calcium 2By similarity
    Metal bindingi152 – 1521Calcium 3By similarity
    Metal bindingi162 – 1621Calcium 1By similarity
    Metal bindingi165 – 1651Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi166 – 1661Calcium 3By similarity
    Metal bindingi167 – 1671Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi170 – 1701Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi172 – 1721Calcium 1By similarity
    Metal bindingi172 – 1721Calcium 3By similarity
    Active sitei203 – 2031NucleophileBy similarity
    Metal bindingi207 – 2071Calcium 1; via carbonyl oxygenBy similarity
    Active sitei228 – 2281Proton donorBy similarity
    Binding sitei230 – 2301SubstrateBy similarity
    Binding sitei292 – 2921SubstrateBy similarity
    Binding sitei311 – 3111SubstrateBy similarity
    Sitei312 – 3121Transition state stabilizerBy similarity
    Binding sitei393 – 3931SubstrateBy similarity
    Binding sitei420 – 4201SubstrateBy 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

    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 1 Publication

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. extracellular region Source: TAIR

    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 – 2424Sequence AnalysisAdd
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    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

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    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.

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 88 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