MULTISPECIES: alpha/beta hydrolase [Listeria].

FASTA View on NCBI
LOCUS       WP_003727925             247 aa            linear   BCT 23-DEC-2024
ACCESSION   WP_003727925
VERSION     WP_003727925.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 247)
  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..247
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..247
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27798
     Region          1..241
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msadrsftlk agnravlllh gfagttedvr elgeilaeng ytvhapnfrg hgdepaiflk
       61 ttpemwyeda vagyrqlekd gyneiaivgv amggvfalkm aesfspkaiv plcanvnrkm
      121 ryipienylt kqlkkqgive qeadqmlkny lpeidvmtea ratfyknvar diekihvptm
      181 igqgcqdeei dadnanyifk hihtndkqlc fyagsghdiv ndcekdilee dliyflddlv
      241 wleekvv