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LOCUS WP_003721422 237 aa linear BCT 24-DEC-2024 ACCESSION WP_003721422 VERSION WP_003721422.1 KEYWORDS RefSeq. SOURCE Listeria ORGANISM Listeria Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae. REFERENCE 1 (residues 1 to 237) AUTHORS Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P. TITLE The ESTHER database on alpha/beta hydrolase fold proteins - An overview of recent developments JOURNAL Chem Biol Interact 383, 110671 (2023) PUBMED 37582413 REFERENCE 2 (residues 1 to 237) AUTHORS Carr,P.D. and Ollis,D.L. TITLE Alpha/beta hydrolase fold: an update JOURNAL Protein Pept Lett 16 (10), 1137-1148 (2009) PUBMED 19508187 REFERENCE 3 (residues 1 to 237) AUTHORS Holmquist,M. TITLE Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms JOURNAL Curr Protein Pept Sci 1 (2), 209-235 (2000) PUBMED 12369917 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10787854 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..237 /organism="Listeria" /db_xref="taxon:1637" Protein 1..237 /product="alpha/beta hydrolase" /EC_number="3.-.-.-" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /calculated_mol_wt=26605 Region 1..232 /region_name="YvaK" /note="Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; COG1647" /db_xref="CDD:441253" ORIGIN 1 mvaclcihgf tgspsevkpl adylrehtdw dvlaptlpgh dhlrhlknvt ykdwivfvds 61 ilsqmlkedd evyiigfsmg gllagwlarh ypevkklvll stavnamewp qlvenskqvl 121 teakevtlkn spmfkryqkk vtetpwtstl qfkkmvalak pvfehieipt fiaqgsadqv 181 vpaeksvnfl mesipgpkel filegskhvi cqdeqadklf aavltflqkd vavlntk