MULTISPECIES: beta-ketoacyl-ACP synthase I [unclassified Vibrio].

LOCUS       WP_017099197             403 aa            linear   BCT 01-SEP-2024
ACCESSION   WP_017099197
VERSION     WP_017099197.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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 :: NF005935.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK07967
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     gene            1..403
                     /gene="fabB"
     Protein         1..403
                     /product="beta-ketoacyl-ACP synthase I"
                     /EC_number="2.3.1.41"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42217
     Region          1..403
                     /region_name="cond_enzymes"
                     /note="Condensing enzymes; Family of enzymes that catalyze
                     a (decarboxylating or non-decarboxylating) Claisen-like
                     condensation reaction. Members are share strong structural
                     similarity, and are involved in the synthesis and
                     degradation of fatty acids, and the...; cl09938"
                     /db_xref="CDD:447866"
     Site            order(105,112..113,117,119..120,132,138,142,146,152,154,
                     156..158,170,173..174,177,198,201..202,261..265,277,390,
                     392)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238430"
     Site            order(161,295,330)
                     /site_type="active"
                     /db_xref="CDD:238430"
ORIGIN      
        1 mkrvvitgmg ivssignnve evlaslkegk sgittseqfk englrsqvwg nlkmnpadhi
       61 drkkmrfmgd aaafaylsme qaiadsglte dqvsndrtgi vagsggassl nqvnavdiir
      121 ekgvkrvgpy mvprtmastv saclatpfki rgvnysmssa catsahcigh ameliqlgkq
      181 dvvfagggee ldwsltmmfd amgalstkyn dtpelasrty dadrdgfvis ggggmlviee
      241 lehavargak iygeivgyga tsdgydmvap sgegavrcmk mamqnvdgvd yvnthgtstp
      301 vgdvkelgai qevfggnspa isatkamtgh algaagvhea iystlmldng fiapsinvan
      361 ldeagegldi vteareqelt tvmsnsfgfg gtnatlvikk yqg