ID   ISDG_STAAR              Reviewed;         107 AA.
AC   Q6GHV0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=SAR1109;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX571856; CAG40111.1; -; Genomic_DNA.
DR   RefSeq; YP_040522.1; -.
DR   SMR; Q6GHV0; 1-107.
DR   GeneID; 2860363; -.
DR   GenomeReviews; BX571856_GR; SAR1109.
DR   KEGG; sar:SAR1109; -.
DR   HOGENOM; Q6GHV0; -.
DR   OMA; Q6GHV0; RDEGTSE.
DR   BioCyc; SAUR282458:SAR1109-MON; -.
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_0000270083.
FT   METAL         7      7       Iron (Potential).
FT   METAL        77     77       Iron (heme axial ligand) (Potential).
FT   SITE         67     67       Transition state stabilizer (Potential).
SQ   SEQUENCE   107 AA;  12546 MW;  DB13A134D5EC4FF0 CRC64;
     MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
     KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK
//