ID K3YSN8_SETIT Unreviewed; 427 AA. AC K3YSN8; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 24-JAN-2024, entry version 66. DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028}; DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|PIRNR:PIRNR001028}; GN Name=101776395 {ECO:0000313|EnsemblPlants:KQL31646}; GN ORFNames=SETIT_1G331000v2 {ECO:0000313|EMBL:RCV08494.1}; OS Setaria italica (Foxtail millet) (Panicum italicum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria. OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV08494.1}; RN [1] {ECO:0000313|EMBL:RCV08494.1, ECO:0000313|Proteomes:UP000004995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL31646, RC ECO:0000313|Proteomes:UP000004995}, and Yugu1 RC {ECO:0000313|EMBL:RCV08494.1}; RX PubMed=22580951; DOI=10.1038/nbt.2196; RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J., RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J., RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X., RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P., RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P., RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.; RT "Reference genome sequence of the model plant Setaria."; RL Nat. Biotechnol. 30:555-561(2012). RN [2] {ECO:0000313|EMBL:RCV08494.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV08494.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:KQL31646} RP IDENTIFICATION. RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL31646}; RG EnsemblPlants; RL Submitted (AUG-2018) to UniProtKB. 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:0000256|ARBA:ARBA00000548, CC ECO:0000256|PIRNR:PIRNR001028, ECO:0000256|RuleBase:RU361134}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913, CC ECO:0000256|PIRNR:PIRNR001028}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028, CC ECO:0000256|RuleBase:RU003615}. 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; AGNK02000566; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CM003528; RCV08494.1; -; Genomic_DNA. DR RefSeq; XP_004954023.1; XM_004953966.1. DR AlphaFoldDB; K3YSN8; -. DR SMR; K3YSN8; -. DR STRING; 4555.K3YSN8; -. DR EnsemblPlants; KQL31646; KQL31646; SETIT_017283mg. DR GeneID; 101776395; -. DR Gramene; KQL31646; KQL31646; SETIT_017283mg. DR KEGG; sita:101776395; -. DR eggNOG; KOG0471; Eukaryota. DR HOGENOM; CLU_030069_1_0_1; -. DR InParanoid; K3YSN8; -. DR OMA; HPFGLAC; -. DR OrthoDB; 201664at2759; -. DR Proteomes; UP000004995; Chromosome I. DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central. 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; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF11; 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 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}; KW Reference proteome {ECO:0000313|Proteomes:UP000004995}; KW Signal {ECO:0000256|PIRNR:PIRNR001028}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|PIRNR:PIRNR001028" FT CHAIN 25..427 FT /note="Alpha-amylase" FT /evidence="ECO:0000256|PIRNR:PIRNR001028" FT /id="PRO_5010604962" FT DOMAIN 25..365 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT DOMAIN 366..426 FT /note="Alpha-amylase C-terminal beta-sheet" FT /evidence="ECO:0000259|SMART:SM00810" FT ACT_SITE 203 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1" FT ACT_SITE 228 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1" SQ SEQUENCE 427 AA; 47500 MW; A9EE9EA4A6D0904B CRC64; MASKGMLLAL FIALLGLSSN SAAGQVLFQG FNWESWKQNG GWYNFLMGKV DDIAEAGITH VWLPPASHSL AEQGYLPGRL YDLDASRYGN EAQLKSLIEA FHDKGVKVIA DIVINHRTAE HQDGRGIYCM FEGGTPDSRL DWGPHMICSD DRAYSDGTGN PDTGADFGGA PDIDHLNPRV QRELIGWLNW LKTDIGFDAW RLDFAKGYSA DVAKVYIDNT EPCFAVAEIW TSLAYGGDGK PYYDQNAHRQ ELVNWVDRVG RSGPATTFDF TTKGILNVAV DGELWRLRGA DGKAPGLIGW WPAKAVTFID NHDTGSTQHM WPFPADKVMQ GYAYILTHPG SPMIFYDHFF DWGLKNEIAH LVSIRDRHGI QPDSELHIIE ADADLYLAEI DGKVIVKIGS RFDCEHLIPE GFHVTAHGDG YAVWEKI //