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Database: UniProt/SWISS-PROT
Entry: AMY1_ARATH
LinkDB: AMY1_ARATH
Original site: AMY1_ARATH 
ID   AMY1_ARATH              Reviewed;         423 AA.
AC   Q8VZ56; Q8LBS5; Q9SW26;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   23-MAY-2018, entry version 110.
DE   RecName: Full=Alpha-amylase 1;
DE            Short=AtAMY1;
DE            EC=3.2.1.1 {ECO:0000269|PubMed:17324226};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=AMY1; OrderedLocusNames=At4g25000; ORFNames=F13M23.140;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INDUCTION.
RX   PubMed=15347792; DOI=10.1104/pp.104.044347;
RA   Smith S.M., Fulton D.C., Chia T., Thorneycroft D., Chapple A.,
RA   Dunstan H., Hylton C., Zeeman S.C., Smith A.M.;
RT   "Diurnal changes in the transcriptome encoding enzymes of starch
RT   metabolism provide evidence for both transcriptional and
RT   posttranscriptional regulation of starch metabolism in Arabidopsis
RT   leaves.";
RL   Plant Physiol. 136:2687-2699(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15637061; DOI=10.1074/jbc.M413638200;
RA   Yu T.S., Zeeman S.C., Thorneycroft D., Fulton D.C., Dunstan H.,
RA   Lue W.L., Hegemann B., Tung S.Y., Umemoto T., Chapple A., Tsai D.L.,
RA   Wang S.M., Smith A.M., Chen J., Smith S.M.;
RT   "alpha-Amylase is not required for breakdown of transitory starch in
RT   Arabidopsis leaves.";
RL   J. Biol. Chem. 280:9773-9779(2005).
RN   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15927942; DOI=10.1093/pcp/pci141;
RA   Kim Y.C., Nakajima M., Nakayama A., Yamaguchi I.;
RT   "Contribution of gibberellins to the formation of Arabidopsis seed
RT   coat through starch degradation.";
RL   Plant Cell Physiol. 46:1317-1325(2005).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=17324226; DOI=10.1111/j.1365-3040.2006.01624.x;
RA   Doyle E.A., Lane A.M., Sides J.M., Mudgett M.B., Monroe J.D.;
RT   "An alpha-amylase (At4g25000) in Arabidopsis leaves is secreted and
RT   induced by biotic and abiotic stress.";
RL   Plant Cell Environ. 30:388-398(2007).
CC   -!- FUNCTION: Possesses alpha-amylase activity in vitro, but seems not
CC       required for breakdown of transitory starch in leaves.
CC       {ECO:0000269|PubMed:17324226}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000269|PubMed:17324226}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P00693};
CC       Note=Binds 3 Ca(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P00693};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305|PubMed:17324226}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and
CC       developing siliques. {ECO:0000269|PubMed:15927942}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during leaf senescence.
CC   -!- INDUCTION: By gibberellin, abscisic acid (ABA), heat shock and
CC       infection with the bacterial pathogen P.syringae. Not regulated by
CC       transition from dark to light. {ECO:0000269|PubMed:15347792,
CC       ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:17324226}.
CC   -!- DISRUPTION PHENOTYPE: Early flowering.
CC       {ECO:0000269|PubMed:15637061}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36742.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035523; CAB36742.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161562; CAB79409.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84990.1; -; Genomic_DNA.
DR   EMBL; AY065233; AAL38709.1; -; mRNA.
DR   EMBL; AY117294; AAM51369.1; -; mRNA.
DR   EMBL; AY087021; AAM64582.1; -; mRNA.
DR   PIR; T05521; T05521.
DR   RefSeq; NP_567714.1; NM_118632.3.
DR   UniGene; At.28556; -.
DR   ProteinModelPortal; Q8VZ56; -.
DR   SMR; Q8VZ56; -.
DR   STRING; 3702.AT4G25000.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; Q8VZ56; -.
DR   PRIDE; Q8VZ56; -.
DR   ProMEX; Q8VZ56; -.
DR   EnsemblPlants; AT4G25000.1; AT4G25000.1; AT4G25000.
DR   GeneID; 828603; -.
DR   Gramene; AT4G25000.1; AT4G25000.1; AT4G25000.
DR   KEGG; ath:AT4G25000; -.
DR   Araport; AT4G25000; -.
DR   TAIR; locus:2117398; AT4G25000.
DR   eggNOG; KOG0471; Eukaryota.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000239525; -.
DR   InParanoid; Q8VZ56; -.
DR   KO; K01176; -.
DR   OMA; GEFWKDS; -.
DR   OrthoDB; EOG093600FS; -.
DR   PhylomeDB; Q8VZ56; -.
DR   BioCyc; ARA:AT4G25000-MONOMER; -.
DR   PRO; PR:Q8VZ56; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8VZ56; baseline and differential.
DR   Genevisible; Q8VZ56; AT.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; TAS:TAIR.
DR   GO; GO:0004556; F:alpha-amylase activity; IMP:TAIR.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR012850; A-amylase_bs_C.
DR   InterPro; IPR013775; A-amylase_pln.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF07821; Alpha-amyl_C2; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00810; Alpha-amyl_C2; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Carbohydrate metabolism; Complete proteome; Glycosidase;
KW   Hydrolase; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    423       Alpha-amylase 1.
FT                                /FTId=PRO_0000418861.
FT   REGION       76     77       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   REGION      201    206       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   REGION      398    400       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    203    203       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   ACT_SITE    228    228       Proton donor.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       116    116       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       133    133       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       136    136       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       138    138       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       142    142       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       152    152       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       162    162       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       166    166       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       167    167       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       170    170       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       172    172       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       172    172       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   METAL       207    207       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04063}.
FT   BINDING     230    230       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     292    292       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     311    311       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     393    393       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     420    420       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   SITE        312    312       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   CONFLICT    419    419       V -> I (in Ref. 4; AAM64582).
FT                                {ECO:0000305}.
SQ   SEQUENCE   423 AA;  47378 MW;  10D2119B6EA572EC CRC64;
     MTSLHTLLFS SLLFFIVFPT FTFSSTLLFQ SFNWESWKKE GGFYNSLHNS IDDIANAGIT
     HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK ALNQKGIKAL ADIVINHRTA
     ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV
     QKELSEWMNW LKTEIGFHGW RFDYVRGYAS SITKLYVQNT SPDFAVGEKW DDMKYGGDGK
     LDYDQNEHRS GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGMIGIM
     PGNAVTFIDN HDTFRTWVFP SDKVLLGYVY ILTHPGTPCI FYNHYIEWGL KESISKLVAI
     RNKNGIGSTS SVTIKAAEAD LYLAMIDDKV IMKIGPKQDV GTLVPSNFAL AYSGLDFAVW
     EKK
//
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