LOCUS       AIG73791.1               401 aa    PRT              BCT 01-OCT-2014
DEFINITION  Amycolatopsis japonica Erythromycin C-12 hydroxylase protein.
ACCESSION   CP008953-850
PROTEIN_ID  AIG73791.1
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="eryK"
                     /locus_tag="AJAP_04345"
                     /EC_number="1.14.13.154"
                     /function="Responsible for the C-12 hydroxylation of the
                     macrolactone ring of erythromycin. Thus, EryK catalyzes
                     the hydroxylation of erythromycin D (ErD) at the C-12
                     position to produce erythromycin C (ErC). Erythromycin B
                     (ErB) is not a substrate for this enzyme."
                     /transl_table=11
BEGIN
        1 MTTIAETWGV HEAQFWLRDE FPADPVRFDA ETGMWNVYGH AEALKTLSDP KVFSSDTTRL
       61 IPKEISPDKD LFVEGNLLQM DPPDHKKLRT LVSHAFTPKV VADLEPRIAA LTNELLDAVD
      121 GADSMELVTH LAYPLPVIVI AELLGIPASD RDLFKEWVDT LLRNSQQRSL IKQTEEDKKA
      181 AEETSAQVKN LVNYLSEHVD DRRRNPREDL LTKLVEAEVD GTKLTQNEVV NFANVLLLAG
      241 HITTTMLLGN TVLCLDSHPD EYRRVRADRT LLPATIEESL RFLSPFALVA RATTTEVELG
      301 GQTIPADSML GIWVAAANRD PRTFTDPGVF DPARAHNPHL AFGRGIHFCI GAPLARLEGK
      361 TALNILLDRF PDLRTDPAVP PSFIPSPHMT GVNELRLLLK P
//