MULTISPECIES: esterase/lipase family protein [Pseudomonas].

LOCUS       WP_003114302             569 aa            linear   BCT 23-DEC-2024
ACCESSION   WP_003114302
VERSION     WP_003114302.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 569)
  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 569)
  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 569)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   4  (residues 1 to 569)
  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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..569
                     /product="esterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0016042 - lipid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63190
     Region          <192..278
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msseplepnq dviiprsrds lgrpvykaql trtdnqsekv alirqtaplp vifipgimgt
       61 nlrnkadkse vwrppnglwp mddlfasiga lwtwawrgpk arqellkaeq vevddqgtid
      121 vgqsglseea arlrgwgkvm rsaynpvmgl merrldnivs rrelqawwnd ealsppgdqg
      181 eeqgkvgpid eeellrasry qfdvwcagyn wlqsnrqsal dvrdyientv lpfyqkecgl
      241 dpeqmrrmkv ilvthsmggl varaltqlhg yervlgvvhg vqpatgssti yhhmrcgyeg
      301 iaqvvlgrna gevtaivans agalelapsa eyregrpwlf lcdaqgqvlk didgkprayp
      361 qnqdpyeeiy knttwyglvp eqnsqyldms dkkeglrvgp rdnfedlids ianfhgelsa
      421 agyhsetyah ygaddsrhsw rdliwkgdpt pletpgatln ddengtynsw frrglptivq
      481 gpletgnpld asgsggdetv ptdsgqapal agvkasfrhg skgkgqantk rgyehqesyn
      541 daraqwaaly gvikitqlad whpndkggt