LOCUS       BAQ46517.1               478 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum dihydrolipoamide dehydrogenase protein.
ACCESSION   AP014704-3137
PROTEIN_ID  BAQ46517.1
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="1.8.1.4"
                     /gene="lpd"
                     /inference="similar to AA sequence:RefSeq:WP_020095323.1"
                     /locus_tag="Maq22A_c16975"
                     /note="180c0011"
                     /note="E3 component of alpha keto acid dehydrogenase
                     complexes LpdC; forms a homodimer; binds one molecule of
                     FAD monomer; catalyzes NAD+-dependent oxidation of
                     dihydrolipoyl cofactors that are covalently linked to the
                     E2 component; Derived by automated computational analysis
                     using gene prediction method: Protein Homology."
                     /transl_table=11
BEGIN
        1 MSDTYDVLII GAGPGGYVAA IRAAQLGFKT AVVDREHLGG ICLNWGCIPT KALLRSAEIY
       61 HYMQHAKDYG LTADNVGFDV SAIVKRSRGV SARLNGGVGM LLKKNKVDVI WGEAAIEVAP
      121 KGDEPGRVVV KETTRAEAPK GAKAAGTYQA KHIVVATGAR PRAIPGIEPD RRQIWTYYEA
      181 MVPERMPKSL LVMGSGAIGI EFASFYRTMG TEVTVVELLP QILPVEDHEI AAHARKRFEK
      241 QGIKILTGAK VTKVAKGDAV TATVETEGGK TQEITAEILI SAVGVVGNIE SLGLEKLGVA
      301 IERGIVATDG LGRTNVPGIY AIGDVAGPPM LAHKAEHEGV ICVETIKGLH THPMDKGKIP
      361 GCTYCQPQIA SVGLTEAKAK EQGFDVRVGR FPFAGNGKAI ALGEPDGLVK TIFDRKTGQL
      421 LGAHMVGAEV TELIQGYVVA MNLETTEEEL MHTVFPHPTL SEMMHESVLD AYGRVIHA
//