AMY3_WHEAT
ID AMY3_WHEAT Reviewed; 413 AA.
AC P08117;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alpha-amylase AMY3;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=AMY1.1; Synonyms=ALPHA-AMY3;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=17186618; DOI=10.1007/bf00329833;
RA Baulcombe D.C., Huttly A.K., Martienssen R.A., Barker R.F., Jarvis M.G.;
RT "A novel wheat alpha-amylase gene (alpha-Amy3).";
RL Mol. Gen. Genet. 209:33-40(1987).
CC -!- FUNCTION: Important for breakdown of endosperm starch during
CC germination.
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 Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P00693};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a high level during germination in
CC the aleurones cells under the control of the plant hormone gibberellic
CC acid and in the developing grains at a low level.
CC -!- MISCELLANEOUS: Binds starch not only at the active site, but also via
CC accessory binding sites on the protein surface that are important for
CC efficient binding to starch granules and thereby increase enzyme
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X05809; CAA29252.1; -; Genomic_DNA.
DR EMBL; M16991; AAA34259.1; -; Genomic_DNA.
DR PIR; S06357; ALWT3.
DR AlphaFoldDB; P08117; -.
DR SMR; P08117; -.
DR STRING; 4565.Traes_5DL_91B56C21D.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P08117; -.
DR EnsemblPlants; TraesCAD_scaffold_111533_01G000300.1; TraesCAD_scaffold_111533_01G000300.1; TraesCAD_scaffold_111533_01G000300.
DR EnsemblPlants; TraesCLE_scaffold_120401_01G000400.1; TraesCLE_scaffold_120401_01G000400.1; TraesCLE_scaffold_120401_01G000400.
DR EnsemblPlants; TraesCS5A02G464500.1; TraesCS5A02G464500.1; TraesCS5A02G464500.
DR EnsemblPlants; TraesPAR_scaffold_072561_01G000200.1; TraesPAR_scaffold_072561_01G000200.1; TraesPAR_scaffold_072561_01G000200.
DR EnsemblPlants; TraesROB_scaffold_058472_01G000200.1; TraesROB_scaffold_058472_01G000200.1; TraesROB_scaffold_058472_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_073930_01G000400.1; TraesWEE_scaffold_073930_01G000400.1; TraesWEE_scaffold_073930_01G000400.
DR Gramene; TraesCAD_scaffold_111533_01G000300.1; TraesCAD_scaffold_111533_01G000300.1; TraesCAD_scaffold_111533_01G000300.
DR Gramene; TraesCLE_scaffold_120401_01G000400.1; TraesCLE_scaffold_120401_01G000400.1; TraesCLE_scaffold_120401_01G000400.
DR Gramene; TraesCS5A02G464500.1; TraesCS5A02G464500.1; TraesCS5A02G464500.
DR Gramene; TraesPAR_scaffold_072561_01G000200.1; TraesPAR_scaffold_072561_01G000200.1; TraesPAR_scaffold_072561_01G000200.
DR Gramene; TraesROB_scaffold_058472_01G000200.1; TraesROB_scaffold_058472_01G000200.1; TraesROB_scaffold_058472_01G000200.
DR Gramene; TraesWEE_scaffold_073930_01G000400.1; TraesWEE_scaffold_073930_01G000400.1; TraesWEE_scaffold_073930_01G000400.
DR eggNOG; KOG0471; Eukaryota.
DR OMA; PGLLGWW; -.
DR BRENDA; 3.2.1.1; 6500.
DR Proteomes; UP000019116; Unplaced.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
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 Calcium; Carbohydrate metabolism; Germination; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..413
FT /note="Alpha-amylase AMY3"
FT /id="PRO_0000001418"
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 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 151
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 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 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 282..284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 385..387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 296
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
SQ SEQUENCE 413 AA; 45370 MW; C262ECA1C54FCCE4 CRC64;
MGKHSATLCG LLVVVLCLAS SLAQAQILFQ GFNWESWKTQ GGWYKFMQGK VEEIASTGAT
HVWLPPPSQS VSPEGYLPGQ LYNLNSKYGS GADLKSLIQA FRGKNISCVA DIVINHRCAD
KKDGRGVYCI FEGGTSDNRL DWGPDEICSD DTKYSNGRGH RDTGGGFDAA PDIDHLNPRV
QRELSAWLNW LKTDLGFDGW RLDFAKGYSA AMAKIYVDNS KPAFVVGELY DRDRQLLANW
VRGVGGPATA FDFPTKGVLQ EAVQGDLGRM RGSDGKAPGM IGWMPEKTVT FIDNHDTGST
QRLWPFPSDK VMQGYAYILT HPGIPCIFYD HVFDWKLKQE ITALATVRSR NGIHPGSTLD
ILKAEGDLYV AKIGGKVITK IGSRYNIGDN VIPSGFKIAA KGNNYCVWEK SGL
