MULTISPECIES: bifunctional 3-hydroxydecanoyl-ACP

LOCUS       WP_000227927             172 aa            linear   BCT 06-NOV-2024
            dehydratase/trans-2-decenoyl-ACP isomerase [Enterobacteriaceae].
ACCESSION   WP_000227927
VERSION     WP_000227927.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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..172
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..172
                     /gene="fabA"
     Protein         1..172
                     /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=18838
     Region          1..172
                     /region_name="PRK05174"
                     /note="bifunctional 3-hydroxydecanoyl-ACP
                     dehydratase/trans-2-decenoyl-ACP isomerase"
                     /db_xref="CDD:179953"
     Site            order(27..29,85,88..89,92..93,104..107)
                     /site_type="active"
                     /note="active site 1 [active]"
                     /db_xref="CDD:238614"
     Site            order(28,30,81,85,104..112,114,116..117)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238614"
     Site            order(78..80,114..117)
                     /site_type="active"
                     /note="active site 2 [active]"
                     /db_xref="CDD:238614"
ORIGIN      
        1 mvdkresytk edllasgrge lfgakgpqlp apnmlmmdrv vkmtetggnf dkgyveaeld
       61 inpdlwffgc hfigdpvmpg clgldamwql vgfylgwlgg egkgralgvg evkftgqvlp
      121 takkvtyrih fkrivnrrli mgladgevlv dgrliytasd lkvglfqdts af