LOCUS       CAQ43773.1               431 aa    PRT              BCT 06-FEB-2015
DEFINITION  Stenotrophomonas maltophilia K279a putative 3-ketoacyl-
            CoA thiolase protein.
ACCESSION   AM743169-155
PROTEIN_ID  CAQ43773.1
SOURCE      Stenotrophomonas maltophilia K279a
  ORGANISM  Stenotrophomonas maltophilia K279a
            Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
            Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia
            group.
REFERENCE   1  (bases 1 to 4851126)
  AUTHORS   Crossman L.C.
  JOURNAL   Submitted (24-MAY-2007) to the INSDC. Crossman L.C., Pathogen
            Sequencing Unit, The Wellcome Trust Sanger Institute, Hinxton,
            Cambridge, Cambridgeshire, CB10 1SA, UNITED KINGDOM.
REFERENCE   2
  AUTHORS   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
            Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N.,
            Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R.,
            Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C.,
            Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
  TITLE     The complete genome, comparative and functional analysis of
            Stenotrophomonas maltophilia reveals an organism heavily shielded
            by drug resistance determinants
  JOURNAL   Genome Biol. 9(4), R74-R74(2008).
   PUBMED   18419807
FEATURES             Qualifiers
     source          /organism="Stenotrophomonas maltophilia K279a"
                     /strain="K279a"
                     /mol_type="genomic DNA"
                     /country="United Kingdom"
                     /db_xref="taxon:522373"
     protein         /transl_table=11
                     /gene="fadI"
                     /locus_tag="Smlt0164"
                     /EC_number="2.3.1.16"
                     /note="similarity:fasta; with=UniProt:P76503
                     (EMBL:AJ586889;); Escherichia coli.; fadI; 3-ketoacyl-CoA
                     thiolase (EC 2.3.1.16) (Fatty acid oxidation complex
                     subunit beta) (Beta-ketothiolase) (Acetyl-CoA
                     acyltransferase) (Acyl- CoA ligase) (ACSs).; length=436;
                     id 38.303%; ungapped id 39.387%; E()=1.2e-53; 436 aa
                     overlap; query 1-430; subject 5-434"
                     /note="similarity:fasta; with=UniProt:Q3BZ84
                     (EMBL:AM039952;); Xanthomonas campestris pv. vesicatoria
                     (strain 85-10).; Acetyl-CoA acyltransferase (EC
                     2.3.1.16).; length=431; id 90.487%; ungapped id 90.487%;
                     E()=7.6e-154; 431 aa overlap; query 1-431; subject 1-431"
                     /db_xref="EnsemblGenomes-Gn:Smlt0164"
                     /db_xref="EnsemblGenomes-Tr:CAQ43773"
                     /db_xref="GOA:B2FHD0"
                     /db_xref="InterPro:IPR002155"
                     /db_xref="InterPro:IPR016039"
                     /db_xref="InterPro:IPR020616"
                     /db_xref="InterPro:IPR020617"
                     /db_xref="UniProtKB/TrEMBL:B2FHD0"
BEGIN
        1 MPGISMPNAR PVAILGGVRI PFCRQNTAYS DVGNLGMSVR TLGALVERFG LHGQQLGEVA
       61 MGAVIKHSSD WNLGREATLS SGLSPLTPGI TLQRACGTSL DSIITVANKI ALGQIESGIG
      121 GGSDTTSDVP IVYGKKLRAR LLAANRAKST GDKIRALTSG FKFSELKPEF PGVAEPRTGK
      181 SMGDHCEDMA KEWNISRDSQ DEWAVSSHKK LAAAYERGFF NDLIAPFRGV ERDNILRPDT
      241 SLEKLATLKP AFDKVSGRGT LTAANSTPLT DGAAAVLLAS EEWARAHGHE PQAYLRDAHV
      301 SAVDFVHGEG LLMAPTVAVP EMLKRNGLTL QDFDIYEIHE AFAAQVLCTL RAWESEDYCR
      361 NRLGLDAPMG RIDPDKINLL GSSLATGHPF AATGARVIAT AAKQLAERGG GRALVSICTA
      421 GGMGVVAIVE R
//