MULTISPECIES: enoyl-ACP reductase FabI [Klebsiella].

LOCUS       WP_004140277             262 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_004140277
VERSION     WP_004140277.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..262
                     /gene="fabI"
     Protein         1..262
                     /product="enoyl-ACP reductase FabI"
                     /EC_number="1.3.1.9"
                     /calculated_mol_wt=27780
     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..107,109..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..107,109..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 itgvasklsi aygiaqamhr egaelaftyq neklkgrvee faaalgsdiv
       61 lpcdvaedes italftelek vwpkfdgfvh sigfapadql dgdyvdvvtr dgfkiahdis
      121 aysfvamaka crgmlnpgsa lltlsylgae raipnynvmg lakasleanv rymanamgpe
      181 gvrvnaisag pirtlaasgi kdfrkmlahc eavtpirrtv tiedvgnsaa flcsnlsagi
      241 sgevvhvdgg fniaamnele lk