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Q8VZ56

- AMY1_ARATH

UniProt

Q8VZ56 - AMY1_ARATH

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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

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
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 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 – 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

« Hide

        10         20         30         40         50
MTSLHTLLFS SLLFFIVFPT FTFSSTLLFQ SFNWESWKKE GGFYNSLHNS
60 70 80 90 100
IDDIANAGIT HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK
110 120 130 140 150
ALNQKGIKAL ADIVINHRTA ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR
160 170 180 190 200
NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV QKELSEWMNW LKTEIGFHGW
210 220 230 240 250
RFDYVRGYAS SITKLYVQNT SPDFAVGEKW DDMKYGGDGK LDYDQNEHRS
260 270 280 290 300
GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGMIGIM
310 320 330 340 350
PGNAVTFIDN HDTFRTWVFP SDKVLLGYVY ILTHPGTPCI FYNHYIEWGL
360 370 380 390 400
KESISKLVAI RNKNGIGSTS SVTIKAAEAD LYLAMIDDKV IMKIGPKQDV
410 420
GTLVPSNFAL AYSGLDFAVW EKK
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

« 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: 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