ID D5DME4_PRIM3 Unreviewed; 483 AA. AC D5DME4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 62. DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ADF42028.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:ADF42028.1}; GN Name=amyL {ECO:0000313|EMBL:ADF42028.1}; GN OrderedLocusNames=BMD_5229 {ECO:0000313|EMBL:ADF42028.1}; OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF42028.1, ECO:0000313|Proteomes:UP000002365}; RN [1] {ECO:0000313|EMBL:ADF42028.1, ECO:0000313|Proteomes:UP000002365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 / IMG 1521 {ECO:0000313|Proteomes:UP000002365}; RX PubMed=21705586; DOI=10.1128/JB.00449-11; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S., RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C., RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J., RA Bremer E., Jahn D., Ravel J., Vary P.S.; RT "Genome sequences of the biotechnologically important Bacillus megaterium RT strains QM B1551 and DSM319."; RL J. Bacteriol. 193:4199-4213(2011). 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; CP001982; ADF42028.1; -; Genomic_DNA. DR RefSeq; WP_013085538.1; NZ_CP120609.1. DR AlphaFoldDB; D5DME4; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; bmd:BMD_5229; -. DR PATRIC; fig|592022.4.peg.5209; -. DR HOGENOM; CLU_024572_2_0_9; -. DR Proteomes; UP000002365; 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:ADF42028.1}; KW Hydrolase {ECO:0000313|EMBL:ADF42028.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}. FT DOMAIN 5..391 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 233 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT ACT_SITE 263 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT BINDING 104 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 196 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 204 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 237 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" SQ SEQUENCE 483 AA; 56090 MW; 872863FBA4031B1E CRC64; MERNHTIMQF FEWHVPADGE HWQRLKELAP QLKEQGIDSV WIPPVTKGVS SEDNGYGVYD LYDLGEFDQK GTVRTKYGTK QELHEAIDAC HNHGINVYVD IVMNHKAAAD EKETFHVIEV DPMNRTEEIS EPFEIEGWTK FTFEGRGDQY SSFKWNFNHF NGTDYDDKNG KEGVFRIAGE NKSWNENVDQ EFGNYDYLMF ANIDYNHPEV REEMIKWGKW LADTLQCDGY RLDAIKHINH DFIKEFAHEL SSSQEKPFYF VGEFWNPELT ACQEFLDVID YQIDLFDVSL HYKLHEASQQ GRDFDLTTIF DDTLVKTHPL NVVTFVDNHD SQPNESLESW VEDWFKQSAY ALILLREDGY PCVFYGDYFG IGGEHPIKGK EKDISALLHV RYDKAYGQQD DYFDHPNTIG WVRHGVEEFE KSGCAVVISN GEDGEKRMFV GEHRSGQTWI DFTNNREDQV VIEEDGYGQF PVNGGSVSVW AEA //