isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.79 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTKDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing) 2

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK

isdI

Heme oxygenase (staphylobilin-producing)

108 amino acids

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.

Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily.

12.791 kDa

MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVRLKSDDDGQQSPILSNKVFKYDIGYHYQK