LOCUS       XP_002555702             378 aa            linear   PLN 11-AUG-2009
DEFINITION  KLTH0G15400p [Lachancea thermotolerans].
ACCESSION   XP_002555702
VERSION     XP_002555702.1  GI:255718843
DBSOURCE    REFSEQ: accession XM_002555656.1
KEYWORDS    .
SOURCE      Lachancea thermotolerans CBS 6340 (Kluyveromyces thermotolerans CBS
            6340)
  ORGANISM  Lachancea thermotolerans CBS 6340
            Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
            Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
REFERENCE   1  (residues 1 to 378)
  CONSRTM   The Genolevures Consortium
  TITLE     Comparative genomics of protoploid Saccharomycetaceae
  JOURNAL   Unpublished
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Genoscope -,C.E.A.
  TITLE     Direct Submission
  JOURNAL   Submitted (04-JUN-2009) Genoscope - Centre National de Sequencage :
            BP 191 91006 EVRY cedex - FRANCE (E-mail : seqref@genoscope.cns.fr
            - Web : www.genoscope.cns.fr)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence is identical to CAR25265.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Lachancea thermotolerans CBS 6340"
                     /strain="CBS 6340"
                     /db_xref="taxon:559295"
                     /chromosome="G"
     Protein         1..378
                     /product="KLTH0G15400p"
                     /calculated_mol_wt=43044
     Region          22..343
                     /region_name="hemH"
                     /note="ferrochelatase; TIGR00109"
                     /db_xref="CDD:211547"
     Region          24..187
                     /region_name="Ferrochelatase_N"
                     /note="Ferrochelatase, N-terminal domain: Ferrochelatase
                     (protoheme ferrolyase or HemH) is the terminal enzyme of
                     the heme biosynthetic pathway. It catalyzes the insertion
                     of ferrous iron into the protoporphyrin IX ring yielding
                     protoheme. This enzyme is...; cd03411"
                     /db_xref="CDD:48638"
     Site            order(30,79,83,92,96,147,150..153,183,185)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:48638"
     Site            order(31,43,47..49,154..155)
                     /site_type="active"
                     /db_xref="CDD:48638"
     Region          192..325
                     /region_name="Ferrochelatase_C"
                     /note="Ferrochelatase, C-terminal domain: Ferrochelatase
                     (protoheme ferrolyase or HemH) is the terminal enzyme of
                     the heme biosynthetic pathway. It catalyzes the insertion
                     of ferrous iron into the protoporphyrin IX ring yielding
                     protoheme. This enzyme is...; cd00419"
                     /db_xref="CDD:73203"
     Site            order(220,225,267,299)
                     /site_type="active"
                     /db_xref="CDD:73203"
     Site            order(231..233,236,240,292,294..296,298,302,325)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:73203"
     CDS             1..378
                     /locus_tag="KLTH0G15400g"
                     /old_locus_tag="KLTH-ORF2973"
                     /coded_by="XM_002555656.1:1..1137"
                     /note="highly similar to uniprot|P16622 Saccharomyces
                     cerevisiae YOR176W HEM15 Ferrochelatase a mitochondrial
                     inner membrane protein catalyzes the insertion of ferrous
                     iron into protoporphyrin IX the eighth and final step in
                     the heme biosynthetic pathway Yfh1p mediates the use of
                     iron by Hem15p"
                     /db_xref="GeneID:8293988"
ORIGIN      
        1 mfraqlpamr afstvgglfq ksptgivfmn mggpstvpet rdflyqlfsd ndlipisrky
       61 qpmiakfisk frtpkiekqy keigggspir kwseyqakrv ceildetcpe taphkpyvaf
      121 ryarpltset yermlkdgvr kaiafsqypq fsysttgssi nelwrqikkl dpertinwsv
      181 idrwptnkgl vkafadnita klqeypedir kdvvllfsah slpmdvintg daypaevgat
      241 vyrvmeqlkf cnpyrlvwqs qvgpkpwlga qtadvtewla psekgliyip iaftsdhiet
      301 lfeidlevig eseykdklkr cdslngsetf iegcadlvke hlesgelysk qlpldfrlgr
      361 ssdtfehpsq vfgdhskk
//