ID   ISDI_STAAR              Reviewed;         108 AA.
AC   Q6GKE0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Heme-degrading monooxygenase isdI;
DE            EC=1.14.99.3;
DE   AltName: Full=Iron-regulated surface determinant isdI;
DE   AltName: Full=Iron-responsive surface determinant isdI;
DE   AltName: Full=Heme oxygenase;
GN   Name=isdI; OrderedLocusNames=SAR0167;
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; CAG39194.1; -; Genomic_DNA.
DR   RefSeq; YP_039632.1; -.
DR   SMR; Q6GKE0; 1-108.
DR   GeneID; 2860322; -.
DR   GenomeReviews; BX571856_GR; SAR0167.
DR   KEGG; sar:SAR0167; -.
DR   HOGENOM; Q6GKE0; -.
DR   OMA; Q6GKE0; DAHSHQG.
DR   BioCyc; SAUR282458:SAR0167-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    108       Heme-degrading monooxygenase isdI.
FT                                /FTId=PRO_0000270084.
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   108 AA;  12790 MW;  8AFA59A571451E0A CRC64;
     MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTKDTDE VKILTIWESE
     DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
//