ID AMYA_VIGMU Reviewed; 421 AA. AC P17859; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 02-SEP-2026, entry version 117. DE RecName: Full=Alpha-amylase; 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; OS Vigna mungo (Black gram) (Phaseolus mungo). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna. OX NCBI_TaxID=3915; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cotyledon; RX PubMed=2377468; DOI=10.1093/nar/18.14.4250; RA Yamauchi D., Minamikawa T.; RT "Nucleotide sequence of cDNA for alpha-amylase from cotyledons of RT germinating Vigna mungo seeds."; RL Nucleic Acids Res. 18:4250-4250(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8290640; DOI=10.1104/pp.103.4.1459; RA Takeuchi H., Yamauchi D., Wada S., Minamikawa T.; RT "Nucleotide sequence of the alpha-amylase gene from Vigna mungo."; RL Plant Physiol. 103:1459-1459(1993). 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 -!- 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}. 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; X53049; CAA37217.1; -; mRNA. DR EMBL; X73301; CAA51734.1; -; Genomic_DNA. DR PIR; S10514; S10514. DR AlphaFoldDB; P17859; -. DR SMR; P17859; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR012850; A-amylase_bs_C. DR InterPro; IPR013775; A-amylase_pln. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013780; Glyco_hydro_b. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. 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; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 2: Evidence at transcript level; KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding; KW Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000305" FT CHAIN 24..421 FT /note="Alpha-amylase" FT /id="PRO_0000001417" FT ACT_SITE 201 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P00693" FT ACT_SITE 226 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 73..74 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 113 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 130 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 149 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 160 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 168 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="1" 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 199..204 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P04063" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 314 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 393 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00693" FT SITE 309 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00693" SQ SEQUENCE 421 AA; 46889 MW; 15CA0DABA3DB4656 CRC64; MDSFSRLSIF CLFISLLPLF SSPALLFQGF NWESSKKGGW YNSLKNSIPD LANAGITHVW LPPPSQSVSP EGYLPGRLYD LDASKYGSKN ELKSLIAAFH EKGIKCLADI VINHRTAERK DGRGIYCIFE GGTPDSRQDW GPSFICRDDT AYSDGTGNND SGEGYDAAPD IDHLNPQVQR ELSEWMNWLK TEIGFDGWRF DFVKGYAPSI SKIYMEQTKP DFAVGEKWDS ISYGQDGKPN YNQDSHRGAL VNWVESAGGA ITAFDFTTKG ILQAAVQGEL WRLIDPNGKP PGMIGVKPEN AVTFIDNHDT GSTQRLWPFP SDKVMQGYAY ILTHPGTPSI FYDHFFDWGL KEQIAKLSSI RLRNGINEKS TVKIMASEGD LYVAKIDNKI MVKIGPKMDL GNLIPSNLHV ATSGQDYAVW E //