ID K3XX03_SETIT Unreviewed; 436 AA. AC K3XX03; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 70. 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=101783371 {ECO:0000313|EnsemblPlants:KQL12203}; GN ORFNames=SETIT_4G278200v2 {ECO:0000313|EMBL:RCV23178.1}, GN SETIT_4G278300v2 {ECO:0000313|EMBL:RCV23179.1}; 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:RCV23178.1}; RN [1] {ECO:0000313|EMBL:RCV23178.1, ECO:0000313|Proteomes:UP000004995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL12203, RC ECO:0000313|Proteomes:UP000004995}, and Yugu1 RC {ECO:0000313|EMBL:RCV23178.1}; 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:RCV23178.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV23178.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:KQL12203} RP IDENTIFICATION. RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL12203}; 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; AGNK02002703; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CM003531; RCV23178.1; -; Genomic_DNA. DR EMBL; CM003531; RCV23179.1; -; Genomic_DNA. DR RefSeq; XP_004966428.1; XM_004966371.1. DR RefSeq; XP_004966429.1; XM_004966372.1. DR AlphaFoldDB; K3XX03; -. DR STRING; 4555.K3XX03; -. DR EnsemblPlants; KQL12203; KQL12203; SETIT_006461mg. DR EnsemblPlants; KQL12204; KQL12204; SETIT_008671mg. DR GeneID; 101782965; -. DR GeneID; 101783371; -. DR Gramene; KQL12203; KQL12203; SETIT_006461mg. DR Gramene; KQL12204; KQL12204; SETIT_008671mg. DR KEGG; sita:101782965; -. DR KEGG; sita:101783371; -. DR eggNOG; KOG0471; Eukaryota. DR HOGENOM; CLU_030069_1_0_1; -. DR InParanoid; K3XX03; -. DR OMA; LNPRTEI; -. DR OrthoDB; 2728918at2759; -. DR Proteomes; UP000004995; Chromosome IV. 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:SF38; ALPHA-AMYLASE ISOZYME 2A; 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..23 FT /evidence="ECO:0000256|PIRNR:PIRNR001028" FT CHAIN 24..436 FT /note="Alpha-amylase" FT /evidence="ECO:0000256|PIRNR:PIRNR001028" FT /id="PRO_5010604957" FT DOMAIN 24..366 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT DOMAIN 367..427 FT /note="Alpha-amylase C-terminal beta-sheet" FT /evidence="ECO:0000259|SMART:SM00810" FT ACT_SITE 202 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1" FT ACT_SITE 227 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1" SQ SEQUENCE 436 AA; 47997 MW; F3284ECA2D0BC407 CRC64; MGMGSRHMCC LSTLLLLLGL SSGQVLFQGF NWESSKQTGG WYNNLMGKVD DIAAAGVTHV WLPPPSHSVS SEGYMPGRLY DLDASKYGTA AELKSLIAAF HDKGVQAVAD IVINHRCADY KDSRGIYCIF EGGTPDSRLD WRAHMICRDD AKYSDGTGNL DTGADFPGAP DIDHLNDRVQ RELTEWMLWL KSDLGFDAWR LDFARGYSAE VARVYINGTA PSFVVAEIWD KMVPAGDDGK PAYDQDPHRQ ALVDWVDKVG GAASPATVFD FTTKGILNAA VEGELWRLID TEGKAPGVIG WWPAKAVTFV DNHDTGSTQA QWPFPHDKVM QGYAYILTHP GNPCIFYDHF FDWGFKDEIA ALVAVRKRNG ITPTSELTIL EHDGDAYVAE IDGKVIVKIG SRYDLGHLIP VGFEVATHGK DYAVWEKGGS EEVTRA //