AMY2_ARATH
ID AMY2_ARATH Reviewed; 413 AA.
AC Q8LFG1; Q9SGS0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable alpha-amylase 2;
DE Short=AtAMY2;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN Name=AMY2; OrderedLocusNames=At1g76130; ORFNames=T23E18.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND 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 [8]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Probable alpha-amylase that does not seem to be required for
CC breakdown of transitory starch in leaves.
CC {ECO:0000269|PubMed:15637061}.
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:0000250|UniProtKB:P00693};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00693};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in developing siliques.
CC {ECO:0000269|PubMed:15927942}.
CC -!- INDUCTION: Circadian-regulated, with a peak in expression at the
CC beginning of the light period. {ECO:0000269|PubMed:15347792}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:15637061}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17626.1; 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; AC009978; AAF17626.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35800.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61100.1; -; Genomic_DNA.
DR EMBL; AK221564; BAD94995.1; -; mRNA.
DR EMBL; BT025560; ABF58978.1; -; mRNA.
DR EMBL; AY084871; AAM61434.1; -; mRNA.
DR PIR; C96789; C96789.
DR RefSeq; NP_001323338.1; NM_001334710.1.
DR RefSeq; NP_177740.1; NM_106262.4.
DR AlphaFoldDB; Q8LFG1; -.
DR SMR; Q8LFG1; -.
DR STRING; 3702.AT1G76130.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q8LFG1; -.
DR PRIDE; Q8LFG1; -.
DR ProteomicsDB; 244404; -.
DR EnsemblPlants; AT1G76130.1; AT1G76130.1; AT1G76130.
DR EnsemblPlants; AT1G76130.2; AT1G76130.2; AT1G76130.
DR GeneID; 843945; -.
DR Gramene; AT1G76130.1; AT1G76130.1; AT1G76130.
DR Gramene; AT1G76130.2; AT1G76130.2; AT1G76130.
DR KEGG; ath:AT1G76130; -.
DR Araport; AT1G76130; -.
DR TAIR; locus:2199808; AT1G76130.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; Q8LFG1; -.
DR OMA; SVAKYYK; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; Q8LFG1; -.
DR BioCyc; ARA:AT1G76130-MON; -.
DR PRO; PR:Q8LFG1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LFG1; baseline and differential.
DR Genevisible; Q8LFG1; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:TAIR.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..413
FT /note="Probable alpha-amylase 2"
FT /id="PRO_0000418862"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 191..196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 286..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 300
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
SQ SEQUENCE 413 AA; 47170 MW; 6825F1BBB4352226 CRC64;
MGYYNNVFDE CNDQTDIGRV IRDGREVILQ AYNWESHKYD WWRNLDGKVP DIAKSGFTSA
WLPPPSQSLA PEGYLPQDLY SLNSAYGSEH LLKSLLRKMK QYKVRAMADI VINHRVGTTR
GHGGMYNRYD GISLPWDEHA VTSCTGGLGN RSTGDNFNGV PNVDHTQHFV RKDIIGWLRW
LRNTVGFQDF RFDFARGYSA NYVKEYIGAA KPLFSVGECW DSCNYNGHGL DYNQDSHRQR
IISWIDATGQ ISAAFDFTTK GILQEAVKGQ YWRLCDAQGK PPGVMGWWPS RAVTFLDNHD
TGSTQAHWPF PSHHVMEGYA YILTHPGIPC VFYDHFYDWG SSIHDQIVKL IDIRRRQDIH
SRSTVRVLKA ESNLYAAIVG EKICMKLGDG SWCPSGRDWT LATSGHRYAV WHK
