LOCUS       BAQ46363.1               424 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum 3-oxoacyl-ACP synthase protein.
ACCESSION   AP014704-2978
PROTEIN_ID  BAQ46363.1
SOURCE      Methylobacterium aquaticum
  ORGANISM  Methylobacterium aquaticum
            Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
            Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (bases 1 to 5348274)
  AUTHORS   Tani,A. and Ogura,Y.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-JAN-2015) to the DDBJ/EMBL/GenBank databases.
            Contact:Akio Tani
            Okayama University, Institute of Plant Science and Resources; Chuo
            2-20-1, Kurashiki, Okayama 710-0046, Japan
REFERENCE   2
  AUTHORS   Tani,A., Ogura,Y., Hayashi,T. and Kimbara,K.
  TITLE     Complete Genome Sequence of Methylobacterium aquaticum Strain 22A,
            Isolated from Racomitrium japonicum Moss
  JOURNAL   Genome Announc 3, e00266-15 (2015)
  REMARK    Publication Status: Online-Only
            DOI:10.1128/genomeA.00266-15
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.7
            Genome Coverage       :: 47x
            Sequencing Technology :: 454 GS FLX; ABI 3730; Illumina PE
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /culture_collection="NBRC:FERM BP-11078"
                     /db_xref="taxon:270351"
                     /mol_type="genomic DNA"
                     /organism="Methylobacterium aquaticum"
                     /strain="MA-22A"
     protein         /EC_number="2.3.1.41"
                     /gene="fabB"
                     /inference="similar to AA sequence:RefSeq:WP_015928546.1"
                     /locus_tag="Maq22A_c16120"
                     /note="5d0012"
                     /note="FabF, beta-Ketoacyl-ACP synthase II, KASII;
                     catalyzes a condensation reaction in fatty acid
                     biosynthesis: addition of an acyl acceptor of two carbons
                     from malonyl-ACP; required for the elongation of
                     short-chain unsaturated acyl-ACP; Derived by automated
                     computational analysis using gene prediction method:
                     Protein Homology."
                     /transl_table=11
BEGIN
        1 MSRDHDAMGR PLVAVTGLGV VTSLGRGVAD NWAALTAGRS GIHAITRFPT EGLRTRIAGT
       61 VDFIAADPMV APMLSERFAE AAADEAVAQA GISGDFPGAL FMAVPPVEIE WPQRQALAEA
      121 AAPNGDVTYA DLLRAAGSRR FDDWHDLFIF GTVADRIADR FGTKGSPISL STACSSGATA
      181 IQLGVEAIRR GEVEAALCIG TDGSVNPESL IRFSLLSALS TQNDPPEAAS KPFAKNRDGF
      241 VMGEGAAALV LESAASARAR GARILGYVLG CGEKGDGFHR TRSSPDGAPI IAAIRAAIDD
      301 AGLHPDQIDT VNAHGTGTPE NDKMEAMGCL AVLGERMRSV PISSNKSMIG HTLTAAGAVE
      361 AAFSLLTIAH GRVPPTLNYA VPDPAIPLDV VTAARDVPVR TVLSNSFGFG GQNTCLIFGA
      421 EPVR
//