ID B8DUR9_BIFA0 Unreviewed; 500 AA. AC B8DUR9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 72. DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ACL29748.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:ACL29748.1}; GN Name=amy {ECO:0000313|EMBL:ACL29748.1}; GN OrderedLocusNames=BLA_1466 {ECO:0000313|EMBL:ACL29748.1}; OS Bifidobacterium animalis subsp. lactis (strain AD011). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL29748.1, ECO:0000313|Proteomes:UP000002456}; RN [1] {ECO:0000313|EMBL:ACL29748.1, ECO:0000313|Proteomes:UP000002456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD011 {ECO:0000313|EMBL:ACL29748.1, RC ECO:0000313|Proteomes:UP000002456}; RX PubMed=19011029; DOI=10.1128/JB.01515-08; RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H., RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.; RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. RT lactis AD011."; RL J. Bacteriol. 191:678-679(2009). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061, 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; CP001213; ACL29748.1; -; Genomic_DNA. DR RefSeq; WP_004217797.1; NC_011835.1. DR AlphaFoldDB; B8DUR9; -. DR STRING; 442563.BLA_1466; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GeneID; 66533296; -. DR KEGG; bla:BLA_1466; -. DR HOGENOM; CLU_024572_2_0_11; -. DR Proteomes; UP000002456; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. 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 InterPro; IPR013776; A-amylase_thermo. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ACL29748.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACL29748.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002456}. FT DOMAIN 9..394 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 236 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT ACT_SITE 266 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT BINDING 109 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 207 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" SQ SEQUENCE 500 AA; 56022 MW; 7173B532435E5BD5 CRC64; MAIDKPNHET MLQCFEWYLP ESHNLWRWLS SQAPSVAHAG FTTAWLPPAY KGQAGDSDVG YGVYDMYDLG EFDAKGSVPT KYGSRMEYLQ AIRAMQGNGV RVFADIVFNH RMGADGTEPV RTHEVNVDDR TRSDSTVVER TLNTVYDFPE RGGVYSTFKW NWSDFTGTDY TTDDGTTGIM RFDGKQWSDN VSHERGNFDY IMGDDVDVNE PEVARELTDW GIWYTTTTGV DGFRLDAVKS IDAGFFAPWL RTMQRYGNHP GIAVGEYWSG DASELTSYLH DCNHCMMLFD VALHFRFEQA SKNPEGFDLR GLAADTLYER EPTYACTFVD NHDTQPGQAL ESWVQPWFKP LAYACILLRD NVLPCVFFGD YYGVPHDLIP PMRFLPHMVW IRAHLLGDQV EAQPGDTAHS LCWVVEGNHP VCVVLNTGSS EVHRQVRNAA LASHTLIDVC HPDAPATTDT QGQGMMRCPP RSCAIYIDAD DYGVMLEALS GTPAAGTVCA //