ID   ISDG_LISMO              Reviewed;         121 AA.
AC   Q92EH3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=lmo0484;
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e / Serovar 1/2a;
RX   MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591975; CAC98563.1; -; Genomic_DNA.
DR   PIR; AE1135; AE1135.
DR   PIR; AG1493; AG1493.
DR   RefSeq; NP_464012.1; -.
DR   RefSeq; YP_002757214.1; -.
DR   GeneID; 7702202; -.
DR   GeneID; 985220; -.
DR   GenomeReviews; AL591824_GR; lmo0484.
DR   KEGG; lmo:lmo0484; -.
DR   ListiList; LMO0484; -.
DR   HOGENOM; Q92EH3; -.
DR   OMA; Q92EH3; DAHSHQG.
DR   BioCyc; LMON169963:LMO0484-MON; -.
DR   BRENDA; 1.14.99.3; 96770.
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    121       Heme-degrading monooxygenase isdG.
FT                                /FTId=PRO_0000270078.
FT   METAL         6      6       Iron (Potential).
FT   METAL        84     84       Iron (heme axial ligand) (Potential).
FT   SITE         74     74       Transition state stabilizer (Potential).
SQ   SEQUENCE   121 AA;  13785 MW;  95674EA508DA2D49 CRC64;
     MIIVTNTIKV EKGAAEHVIR QFTGANGDGH PTKDIAEVEG FLGFELWHSK PEDKDYEEVV
     VTSKWESEEA QRNWVKSDSF KKAHGRTKDT REQREDRKGI VGNAIARFEV VHVQNPVIVE
     K
//