enoyl-ACP reductase FabI [Listeria monocytogenes].

LOCUS       WP_010989630             262 aa            linear   BCT 11-APR-2024
ACCESSION   WP_010989630
VERSION     WP_010989630.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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 :: NF006369.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK08594
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..262
                     /gene="fabI"
     Protein         1..262
                     /product="enoyl-ACP reductase FabI"
                     /EC_number="1.3.1.-"
                     /GO_function="GO:0004318 - enoyl-[acyl-carrier-protein]
                     reductase (NADH) activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28163
     Region          1..261
                     /region_name="PRK08594"
                     /note="enoyl-[acyl-carrier-protein] reductase FabI"
                     /db_xref="CDD:236308"
     Site            order(14..16,20..21,41,68..70,96..99,123,150..152,162,169,
                     195..198,200..203)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187630"
     Site            order(31,70..73,76,108..114,117..118,121..122,125..126,
                     129,133,136,154..155,157..160,162..163,166..167,170..171,
                     174..175,177..182,184..185,212,215,221..224,230,233..234,
                     237,242,244..256,258..261)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187630"
     Site            order(70..73,108..114,117..118,121..122,125..126,129,
                     132..133,136,154..155,157..159,162..163,166..167,170..171,
                     174..175,177..179,181..183)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187630"
     Site            order(98,100,152,162,165,169,202..203,206,209)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187630"
     Site            order(124,152,165,169)
                     /site_type="active"
                     /db_xref="CDD:187630"
ORIGIN      
        1 mnlslegkty vvmgvankrs iawaiarsln eagaklvfty addrakksit elvpslsevn
       61 qnplilacdv tseeaitetf etikdkagkl sglahciafa nkdfltgdyl evdrksflqa
      121 heisaysfta varalkhlem ltedaslltl tylggervve nynimgvaka sldasvryla
      181 mdlgaigvrv naisagpirt vsargvsgfs dsislveera plkratqaee vgdtayylfs
      241 nlsrgvtgev ihvdsgyhii gf