ID B7IQL5_BACC2 Unreviewed; 513 AA. AC B7IQL5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 73. DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ACK98086.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:ACK98086.1}; GN Name=amyS {ECO:0000313|EMBL:ACK98086.1}; GN OrderedLocusNames=BCG9842_B1758 {ECO:0000313|EMBL:ACK98086.1}; OS Bacillus cereus (strain G9842). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK98086.1, ECO:0000313|Proteomes:UP000006744}; RN [1] {ECO:0000313|EMBL:ACK98086.1, ECO:0000313|Proteomes:UP000006744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842 {ECO:0000313|EMBL:ACK98086.1, RC ECO:0000313|Proteomes:UP000006744}; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; 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; CP001186; ACK98086.1; -; Genomic_DNA. DR RefSeq; WP_000476900.1; NC_011772.1. DR AlphaFoldDB; B7IQL5; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; bcg:BCG9842_B1758; -. DR HOGENOM; CLU_024572_2_0_9; -. DR Proteomes; UP000006744; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1. DR Gene3D; 2.40.30.140; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013776; A-amylase_thermo. DR InterPro; IPR015237; Alpha-amylase_C_pro. 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:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF09154; Alpha-amy_C_pro; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 4: Predicted; KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2}; KW Glycosidase {ECO:0000313|EMBL:ACK98086.1}; KW Hydrolase {ECO:0000313|EMBL:ACK98086.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}. FT DOMAIN 33..421 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 261 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT ACT_SITE 291 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 211 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 230 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 232 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 330 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 437 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 460 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" SQ SEQUENCE 513 AA; 58257 MW; 996A046272F87204 CRC64; MFKRVTIVGL SVVMFLPSIY EGSKAYADTV NNGTLMQYFE WYAPNDGDHW NRLRTDAENL AQKGITSVWI PPAYKGTTQN DVGYGAYDLY DLGEFNQKGT VRTKYGTKAQ LKSAIDALHK KNIDVYGDVV MNHKGGADYT ETVTAVEVDP SNRNVEVSGD YEISAWTGFN FPGRGDSYSN FKWKWYHFDG TDWDEGKKLN RIYKFRGIGK AWDWEVSSEN GNYDYLMYAD LDFDHPDVAN EMKKWGTWYA KELNLDGFRL DAVKHIDHEY LRDWVNHVRQ QTGKEMFTVA EYWQNDIQTL NNYLAKVNYN QSVFDAPLHY NFQYASTGNG NYDMRNILKG TVVANHPTLA VTLVENHDSQ PGQSLESVVS PWFKPLAYAF ILTRAEGYPS VFYGDYYGTK GNSNYEIPAL KDKIDPILTA RKNFAYGTQR DYFDHPDVIG WTREGDSVHA NSGLATLISD GPGGSKWMDV GKNNAGEVWY DITGNQTNTV TINKDGWGQF QVSGGSVSIY VQQ //