ID   ISDG_BACAH              Reviewed;         107 AA.
AC   A0RJE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Heme-degrading monooxygenase isdG;
DE            EC=1.14.99.3;
DE   AltName: Full=Iron-regulated surface determinant isdG;
DE   AltName: Full=Iron-responsive surface determinant isdG;
DE   AltName: Full=Heme oxygenase;
GN   Name=isdG; OrderedLocusNames=BALH_4126;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Allows bacterial pathogens to use the host heme as an
CC       iron source. Catalyzes the oxidative degradation of the heme
CC       macrocyclic porphyrin ring in the presence of a suitable electron
CC       donor such as ascorbate or NADPH--cytochrome P450 reductase, with
CC       subsequent release of free iron (By similarity).
CC   -!- CATALYTIC ACTIVITY: Heme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+)
CC       + CO + 3 A + 3 H(2)O.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. Heme-degrading monooxygenase isdG subfamily.
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DR   EMBL; CP000485; ABK87336.1; -; Genomic_DNA.
DR   RefSeq; YP_896843.1; -.
DR   GeneID; 4544515; -.
DR   GenomeReviews; CP000485_GR; BALH_4126.
DR   KEGG; btl:BALH_4126; -.
DR   OMA; A0RJE3; DAHSHQG.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:HAMAP.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:EC.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01272; -; 1.
DR   InterPro; IPR007138; Antibiotic_mOase.
DR   Pfam; PF03992; ABM; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN         1    107       Heme-degrading monooxygenase isdG.
FT                                /FTId=PRO_1000067382.
FT   METAL         6      6       Iron (Potential).
FT   METAL        76     76       Iron (heme axial ligand) (Potential).
FT   SITE         66     66       Transition state stabilizer (Potential).
SQ   SEQUENCE   107 AA;  12004 MW;  ACB308A337A92DFB CRC64;
     MIIVTNTAKI TKGNGHKLID RFNKVGQVET MPGFLGLEVL LTQNTVDYDE VTISTRWNAK
     EDFQGWTKSP AFKAAHSHQG GMPDYILDNK ISYYDVKVVR MPMAAAQ
//