bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP

LOCUS       WP_001018747             208 aa            linear   BCT 06-NOV-2024
            isomerase [Escherichia coli].
ACCESSION   WP_001018747
VERSION     WP_001018747.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 :: NF003509.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05174
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..208
                     /gene="fabA"
     Protein         1..208
                     /product="bifunctional 3-hydroxydecanoyl-ACP
                     dehydratase/trans-2-decenoyl-ACP isomerase"
                     /EC_number="4.2.1.59"
                     /EC_number="5.3.3.14"
                     /GO_function="GO:0019171 -
                     (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22934
     Region          37..208
                     /region_name="PRK05174"
                     /note="bifunctional 3-hydroxydecanoyl-ACP
                     dehydratase/trans-2-decenoyl-ACP isomerase"
                     /db_xref="CDD:179953"
     Site            order(63..65,121,124..125,128..129,140..143)
                     /site_type="active"
                     /note="active site 1 [active]"
                     /db_xref="CDD:238614"
     Site            order(64,66,117,121,140..148,150,152..153)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238614"
     Site            order(114..116,150..153)
                     /site_type="active"
                     /note="active site 2 [active]"
                     /db_xref="CDD:238614"
ORIGIN      
        1 maitlaelvy seliglvqrt rvsypacfnk irltenmvdk resytkedll asgrgelfga
       61 kgpqlpapnm lmmdrvvkmt etggnfdkgy veaeldinpd lwffgchfig dpvmpgclgl
      121 damwqlvgfy lgwlggegkg ralgvgevkf tgqvlptakk vtyrihfkri vnrrlimgla
      181 dgevlvdgrl iytasdlkvg lfqdtsaf