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 03-AUG-2022, entry version 126.
DE RecName: Full=Alpha-amylase 1 {ECO:0000303|PubMed:15347792};
DE Short=AtAMY1 {ECO:0000303|PubMed:15347792};
DE EC=3.2.1.1 {ECO:0000269|PubMed:17324226};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000303|PubMed:17324226};
DE Flags: Precursor;
GN Name=AMY1 {ECO:0000303|PubMed:15347792};
GN OrderedLocusNames=At4g25000 {ECO:0000312|Araport:AT4G25000};
GN ORFNames=F13M23.140 {ECO:0000312|EMBL:CAB36742.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., 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., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis 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 reference
RT 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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., Dunstan H.,
RA Hylton C., Zeeman S.C., Smith A.M.;
RT "Diurnal changes in the transcriptome encoding enzymes of starch metabolism
RT provide evidence for both transcriptional and posttranscriptional
RT regulation of starch metabolism in Arabidopsis 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., Lue W.L.,
RA Hegemann B., Tung S.Y., Umemoto T., Chapple A., Tsai D.L., Wang S.M.,
RA 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 coat
RT 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 induced
RT by biotic and abiotic stress.";
RL Plant Cell Environ. 30:388-398(2007).
RN [9]
RP INDUCTION BY NAC072/RD26.
RC STRAIN=cv. Columbia;
RX PubMed=29659022; DOI=10.1111/nph.15127;
RA Kamranfar I., Xue G.-P., Tohge T., Sedaghatmehr M., Fernie A.R.,
RA Balazadeh S., Mueller-Roeber B.;
RT "Transcription factor RD26 is a key regulator of metabolic reprogramming
RT during dark-induced senescence.";
RL New Phytol. 218:1543-1557(2018).
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:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={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. {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 developing
CC 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. Triggered by NAC072/RD26 during
CC senescence (PubMed:29659022). {ECO:0000269|PubMed:15347792,
CC ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:17324226,
CC ECO:0000269|PubMed:29659022}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. {ECO:0000269|PubMed:15637061}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; 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 ProteomicsDB; 245051; -.
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 HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; Q8VZ56; -.
DR OMA; HPFGLAC; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; Q8VZ56; -.
DR BioCyc; ARA:AT4G25000-MON; -.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
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; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..423
FT /note="Alpha-amylase 1"
FT /id="PRO_0000418861"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 201..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 398..400
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 312
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT CONFLICT 419
FT /note="V -> I (in Ref. 4; AAM64582)"
FT /evidence="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
