MULTISPECIES: hotdog fold thioesterase [Pseudomonas].

LOCUS       WP_003087490             145 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_003087490
VERSION     WP_003087490.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Leduc,D., Battesti,A. and Bouveret,E.
  TITLE     The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal
            enterobactin biosynthesis by interacting with the ArCP domain of
            EntB
  JOURNAL   J. Bacteriol. 189 (19), 7112-7126 (2007)
   PUBMED   17675380
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J. Biol. Chem. 281 (16), 11028-11038 (2006)
   PUBMED   16464851
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  :: HMM
            Evidence Accession :: TIGR00369.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..145
                     /product="hotdog fold thioesterase"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15464
     Region          3..138
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Site            order(54,84,91..94)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(55,57,60,85..89,91)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(56,64..65,68..69,84)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 mslwrqtpdl eqlnasqkns igdllgirfe afddesltas mpvdsrthqp fgllhggasv
       61 vlaeslgsma sylcvdtsqy ycvglevnan hlrglrsgrv tavaraihlg rtthvwdirl
      121 sgddgkpsci arltmavvpl agrag