LOCUS       AIG80238.1               308 aa    PRT              BCT 01-OCT-2014
DEFINITION  Amycolatopsis japonica Delta-aminolevulinic acid dehydratase
            protein.
ACCESSION   CP008953-7297
PROTEIN_ID  AIG80238.1
SOURCE      Amycolatopsis japonica
  ORGANISM  Amycolatopsis japonica
            Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
            Amycolatopsis; Amycolatopsis japonica group.
REFERENCE   1  (bases 1 to 8961318)
  AUTHORS   Stegmann,E., Albersmeier,A., Spohn,M., Gert,H., Weber,T.,
            Wohlleben,W., Kalinowski,J. and Ruckert,C.
  TITLE     Complete genome sequence of the actinobacterium Amycolatopsis
            japonica MG417-CF17(T) (=DSM 44213T) producing
            (S,S)-N,N'-ethylenediaminedisuccinic acid
  JOURNAL   J. Biotechnol. (2014) In press
   PUBMED   25193710
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (bases 1 to 8961318)
  AUTHORS   Ruckert,C., Stegmann,E., Spohn,M., Gert,H., Weber,T., Wohlleben,W.
            and Kalinowski,J.
  TITLE     Direct Submission
  JOURNAL   Submitted (17-JUL-2014) CeBiTec, Bielefeld University,
            Universitaetsstr. 27, Bielefeld, NRW 33615, Germany
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.5.3
            Genome Coverage       :: 23.56x
            Sequencing Technology :: 454
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /organism="Amycolatopsis japonica"
                     /mol_type="genomic DNA"
                     /strain="MG417-CF17"
                     /isolation_source="soil"
                     /culture_collection="DSM:44213"
                     /type_material="type strain of Amycolatopsis japonica"
                     /db_xref="taxon:208439"
                     /country="Japan"
     protein         /gene="hemB"
                     /locus_tag="AJAP_37205"
                     /EC_number="4.2.1.24"
                     /function="Catalyzes an early step in the biosynthesis of
                     tetrapyrroles. Binds two molecules of 5-aminolevulinate
                     per subunit, each at a distinct site, and catalyzes their
                     condensation to form porphobilinogen (By similarity)."
                     /transl_table=11
BEGIN
        1 MRRLVGETTL RPRQLILPMF VAEGADTPRP ISSMPGVVQH TRDTLRKAAV EAVNAGVGGL
       61 MLFGIPKTRD AEGSGAIDPN GILNVALRDL RSELGDATVL MADTCLDEFT DHGHCGVLDA
      121 DGGVDNDATL RVYAEMALAQ VEAGAHLLGP SGMMDGQVGV IRGALDRAGH TDAGILAYSA
      181 KFASAFYGPF REAVDSQLKG DRKTYQQDPG NVREALREIE LDIAEGADMV MVKPALSYLD
      241 VIRAAAEASP VPVAAYNISG EYAMVEAAAA NGWLDRERTI LEVLTSIRRA GADMILTYWA
      301 AEAAAWLD
//