ID Q6HFU3_BACHK Unreviewed; 513 AA. AC Q6HFU3; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 98. DE SubName: Full=Alpha-amylase (1,4-alpha-D-glucan glucanohydrolase) {ECO:0000313|EMBL:AAT60457.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:AAT60457.1}; GN Name=amyS {ECO:0000313|EMBL:AAT60457.1}; GN OrderedLocusNames=BT9727_3261 {ECO:0000313|EMBL:AAT60457.1}; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60457.1, ECO:0000313|Proteomes:UP000001301}; RN [1] {ECO:0000313|EMBL:AAT60457.1, ECO:0000313|Proteomes:UP000001301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27 {ECO:0000313|EMBL:AAT60457.1, RC ECO:0000313|Proteomes:UP000001301}; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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; AE017355; AAT60457.1; -; Genomic_DNA. DR RefSeq; WP_011181796.1; NC_005957.1. DR RefSeq; YP_037583.1; NC_005957.1. DR AlphaFoldDB; Q6HFU3; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; btk:BT9727_3261; -. DR PATRIC; fig|281309.8.peg.3476; -. DR HOGENOM; CLU_024572_2_0_9; -. DR Proteomes; UP000001301; 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:AAT60457.1}; KW Hydrolase {ECO:0000313|EMBL:AAT60457.1}; 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; 58342 MW; CA9683F6C31A26C3 CRC64; MFKKITIVGL SVVLFLPSIY GGSKVYADTI NNGTLMQYFE WYAPSDGNHW NRLRTDAENL AQKGITSVWI PPAYKGTTQN DVGYGAYDLY DLGEFNQKGT VRTKYGTKAQ LKSAIEALHK QNIDVYGDVV MNHKGGADYT ETVTAVEVDR NNRNVEVSGD YEISAWTGFN FPGRGDNYSN FKWKWYHFDG TDWDEGRKLN RIYKFRGIGK AWDWEVSSEN GNYDYLMYAD LDFDHPDVAN EMKNWGTWYA NELNLDGFRL DAVKHIDHEY LRDWVNHVRQ QTRKEMFTVA EYWQNDIHTL NNYLAKVNYN QSVFDAPLHY NFHYASKGNG NYDMRNILNG TVMQNHPALA VTLVENHDSQ PGQSLESVVS AWFKPLAYGF ILTRAEGYPS VFYGDYYGTS GNSSYEIPAL KDKIDPILTA RKNFAYGTQR DYLDHPDVIG WTREGDSVHA NSGLATLISD GPGGSKWMDV GKNNAGEVWH DMTGNQTNTV TINKDGWGQF HVSGGSVSIY VQQ //