MULTISPECIES: enoyl-ACP reductase FabI [Enterobacteriaceae].

LOCUS       WP_000506490             262 aa            linear   BCT 16-DEC-2020
ACCESSION   WP_000506490
VERSION     WP_000506490.1
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 :: NF005938.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK07984
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..262
                     /gene="fabI"
     Protein         1..262
                     /product="enoyl-ACP reductase FabI"
                     /EC_number="1.3.1.9"
                     /calculated_mol_wt=27733
     Region          1..262
                     /region_name="PRK07984"
                     /note="enoyl-ACP reductase FabI"
                     /db_xref="CDD:181187"
     Site            order(13..15,19..20,40,63..65,91..94,119,144..146,156,163,
                     189..192,194..197)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187630"
     Site            order(30,65..68,71,103..106,108..110,113..114,117..118,
                     121..122,125,129,132,148..149,151..154,156..157,160..161,
                     164..165,168..169,171..176,178..179,206,209,215..218,224,
                     227..228,231,236,238..250,252..253)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187630"
     Site            order(65..68,103..106,108..110,113..114,117..118,121..122,
                     125,128..129,132,148..149,151..153,156..157,160..161,
                     164..165,168..169,171..173,175..177)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187630"
     Site            order(93,95,146,156,159,163,196..197,200,203)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187630"
     Site            order(120,146,159,163)
                     /site_type="active"
                     /db_xref="CDD:187630"
ORIGIN      
        1 mgflsgkril vtgvasklsi aygiaqamhr egaelaftyq ndklkgrvee faaqlgsdiv
       61 lqcdvaedas idtmfaelgk vwpkfdgfvh sigfapgdql dgdyvnavtr egfkiahdis
      121 sysfvamaka crsmlnpgsa lltlsylgae raipnynvmg lakasleanv rymanamgpe
      181 gvrvnaisag pirtlaasgi kdfrkmlahc eavtpirrtv tiedvgnsaa flcsdlsagi
      241 sgevvhvdgg fsiaamnele lk