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Heme oxygenase (staphylobilin-producing) 1 (EC 1.14.99.48) (Heme-degrading monooxygenase 1) (Iron-regulated surface determinant 1) (Iron-responsive surface determinant 1)

 HDOX1_STAAM             Reviewed;         107 AA.
Q99UW8;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
07-JUN-2017, entry version 92.
RecName: Full=Heme oxygenase (staphylobilin-producing) 1 {ECO:0000255|HAMAP-Rule:MF_01272};
EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
AltName: Full=Heme-degrading monooxygenase 1 {ECO:0000255|HAMAP-Rule:MF_01272};
AltName: Full=Iron-regulated surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
AltName: Full=Iron-responsive surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
Name=isdG; OrderedLocusNames=SAV1136;
Staphylococcus aureus (strain Mu50 / ATCC 700699).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=158878;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Mu50 / ATCC 700699;
PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
Ogasawara N., Hayashi H., Hiramatsu K.;
"Whole genome sequencing of meticillin-resistant Staphylococcus
aureus.";
Lancet 357:1225-1240(2001).
-!- FUNCTION: Allows bacterial pathogens to use the host heme as an
iron source. Catalyzes the oxidative degradation of the heme
macrocyclic porphyrin ring to the oxo-bilirubin chromophore
staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-
bilirubin and 15-oxo-beta-bilirubin) in the presence of a suitable
electron donor such as ascorbate or NADPH--cytochrome P450
reductase, with subsequent release of free iron.
{ECO:0000255|HAMAP-Rule:MF_01272}.
-!- CATALYTIC ACTIVITY: Protoheme + 5 reduced acceptor + 4 O(2) = 5-
oxo-delta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4
H(2)O. {ECO:0000255|HAMAP-Rule:MF_01272}.
-!- CATALYTIC ACTIVITY: Protoheme + 5 reduced acceptor + 4 O(2) = 15-
oxo-beta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01272}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
-!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
family. Heme-degrading monooxygenase IsdG subfamily.
{ECO:0000255|HAMAP-Rule:MF_01272}.
-!- SEQUENCE CAUTION:
Sequence=BAB57298.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; BA000017; BAB57298.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_000670950.1; NC_002758.2.
ProteinModelPortal; Q99UW8; -.
SMR; Q99UW8; -.
STRING; 158878.SAV1136; -.
PaxDb; Q99UW8; -.
EnsemblBacteria; BAB57298; BAB57298; SAV1136.
GeneID; 31213893; -.
KEGG; sav:SAV1136; -.
eggNOG; COG2329; LUCA.
HOGENOM; HOG000008026; -.
KO; K07145; -.
OMA; IVTIMTT; -.
PhylomeDB; Q99UW8; -.
Proteomes; UP000002481; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0033212; P:iron assimilation; IEA:InterPro.
HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
InterPro; IPR007138; ABM_dom.
InterPro; IPR011008; Dimeric_a/b-barrel.
InterPro; IPR023953; IsdG.
Pfam; PF03992; ABM; 1.
SUPFAM; SSF54909; SSF54909; 1.
PROSITE; PS51725; ABM; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase.
CHAIN 1 107 Heme oxygenase (staphylobilin-producing)
1.
/FTId=PRO_0000270087.
DOMAIN 3 92 ABM. {ECO:0000255|HAMAP-Rule:MF_01272}.
REGION 22 29 Heme binding. {ECO:0000255|HAMAP-
Rule:MF_01272}.
METAL 7 7 Iron. {ECO:0000255|HAMAP-Rule:MF_01272}.
METAL 77 77 Iron (heme axial ligand).
{ECO:0000255|HAMAP-Rule:MF_01272}.
SITE 67 67 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01272}.
SEQUENCE 107 AA; 12546 MW; DB13A134D5EC4FF0 CRC64;
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK


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