ID B1YLA5_EXIS2 Unreviewed; 486 AA. AC B1YLA5; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 93. DE SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:ACB60337.1}; GN OrderedLocusNames=Exig_0857 {ECO:0000313|EMBL:ACB60337.1}; 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:ACB60337.1, ECO:0000313|Proteomes:UP000001681}; RN [1] {ECO:0000313|EMBL:ACB60337.1, 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:ACB60337.1, 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; ACB60337.1; -; Genomic_DNA. DR RefSeq; WP_012369761.1; NC_010556.1. DR AlphaFoldDB; B1YLA5; -. DR STRING; 262543.Exig_0857; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; esi:Exig_0857; -. 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}. 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 486 AA; 56314 MW; BF749DD6EE4D2D70 CRC64; MERNHTMMQF FEWHVENDGK HWQRLKERAP ELRAAGITSV WIPPASKGQS DEDTGYGIYD VYDLGEFDQK GTVRTKYGTK DELIEAIQVA HENDIAVYAD VVMNHKAAAD ELETINVVEV HPEDRSKEIS EEFEIEAWTK FTFPGRNGKY SDFIWTHEFF NGTDFDAREE KTGVFKISGK NKDWNDQVDN EFGNYDYLMF ANIDYNHPEV REEMINWGNW FKETINCQGF RLDAIKHINY EFVNEFAKSM IGDDPDGFYM VGEFWKSDLD DCRQFLDSVD YTIDLFDVPL HYKFHEASQQ GQDFDLTTLF ADTLVESHPT NAVTFVDNHD SQPGESLESW IDDWFKQHAY ASVLLRKDGY PCVFYGDYYG VQGPHPVEGK KEMIDALLYT RYHKAYGEQE DYMDDAHCVG WVRRGVEEFP NSGCAVLLSN ADMCEKRMFV GETRAGEEWF DYTNHQEEPV VIDEEGFGVF PVPGGGVSVF APRDEQ //