ID   ISDG_STAA1              Reviewed;         108 AA.
AC   A7WXE5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
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=SAHV_0164;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17954695; DOI=10.1128/AAC.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic
RT   conversion of Staphylococcus aureus from heterogeneous vancomycin-
RT   intermediate resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF77047.1; -; Genomic_DNA.
DR   RefSeq; YP_001440754.1; -.
DR   GeneID; 5560433; -.
DR   GenomeReviews; AP009324_GR; SAHV_0164.
DR   KEGG; saw:SAHV_0164; -.
DR   OMA; A7WXE5; 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    108       Heme-degrading monooxygenase isdG.
FT                                /FTId=PRO_1000067384.
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;  12791 MW;  8AF2718571451004 CRC64;
     MFMAENRLQL QKGSAEETIE RFYNRQGIET IEGFQQMFVT KTLNTEDTDE VKILTIWESE
     DSFNNWLNSD VFKEAHKNVR LKSDDDGQQS PILSNKVFKY DIGYHYQK
//