ID B1YLX3_EXIS2 Unreviewed; 513 AA. AC B1YLX3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 94. DE SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:ACB60456.1}; GN OrderedLocusNames=Exig_0976 {ECO:0000313|EMBL:ACB60456.1}; OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 / OS 255-15). OC Bacteria; Bacillota; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB60456.1, ECO:0000313|Proteomes:UP000001681}; RN [1] {ECO:0000313|EMBL:ACB60456.1, ECO:0000313|Proteomes:UP000001681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15 RC {ECO:0000313|Proteomes:UP000001681}; RX PubMed=16489412; DOI=10.1007/s00792-005-0497-5; RA Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D., RA Thomashow M.F., Tiedje J.M.; RT "Characterization of Exiguobacterium isolates from the Siberian permafrost. RT Description of Exiguobacterium sibiricum sp. nov."; RL Extremophiles 10:285-294(2006). RN [2] {ECO:0000313|EMBL:ACB60456.1, ECO:0000313|Proteomes:UP000001681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15 RC {ECO:0000313|Proteomes:UP000001681}; RX PubMed=19019206; DOI=10.1186/1471-2164-9-547; RA Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.; RT "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain RT isolated from 3 million year old permafrost: a genome and transcriptome RT approach."; RL BMC Genomics 9:547-547(2008). RN [3] {ECO:0000313|Proteomes:UP000001681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15 RC {ECO:0000313|Proteomes:UP000001681}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."; RL Submitted (APR-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; CP001022; ACB60456.1; -; Genomic_DNA. DR RefSeq; WP_012369880.1; NC_010556.1. DR AlphaFoldDB; B1YLX3; -. DR SMR; B1YLX3; -. DR STRING; 262543.Exig_0976; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; esi:Exig_0976; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_024572_2_0_9; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000001681; Chromosome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001681}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..30 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 31..513 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5039155905" 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; 57606 MW; 9816F477C3FEEC8E CRC64; MKQKRLIVAT LATATFLAPL VQPIAVGATA DNGTMMQYFE WYVPNDGNHW NRLGSDSTKL DQLGITSVWI PPAYKGTTQN DVGYGAYDLY DLGEFNQKGT VRTKYGTKAQ LKTAINQLHT AGIDVYGDVV MNHKGGADFT EAVTAVEVNG SNRNQEISGD YQIQAWTGFD FAARNNTYSN FKWKWYHFDG TDWDQSRSKS AIYKFRGTGK AWDTDVSTEN GNYDYLMYAD IDFDHPEVQQ EMKNWGKWYV NELGLDGFRL DAVKHIKHGY LADWLANVRQ TTGKPLFTVA EYWQNDLGTL QNYLSRTNYQ QSVFDAPLHY KFEQASKGGG YYDMRTIFDG TLVKTNPVQA VTLVENHDSQ PGQSLESTVQ SWFKPLAYAM ILTREQGYPS VFYGDYYGTK GTSNREIPAL ASKIDPLLKA RKDFAFGKQN DYLDNADVIG WTREGVTDRA KSGLATILSD GPGGSKWMYV GLQNKGEVWT DITGNNTASV TINQDGYGQF FVNGGSVSVY RQQ //