isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.785 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK

isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.785 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK

isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.785 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK

isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.785 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK

isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.785 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNAIARFEVVHVQNPVIVEK

isdG

Heme-degrading monooxygenase

121 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 biliverdin 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.

13.845 kDa

MIIVTNTIKVEKGAAEHVIRQFTGANGDGHPTKDIAEVEGFLGFELWHSKPEDKDYEEVVVTSKWESEEAQRNWVKSDSFKKAHGRTKDTREQREDRKGIVGNEIARFEVVHVQNPVTIEK

isdG

Heme-degrading monooxygenase

116 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 biliverdin 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.

13.175 kDa

MVIVTNTSKITKGNGEKLIERFNKVGKVEFMEGFLGLEVLLTENTKDFDEVTVVTRWNTKDDFKNWTKSSAFRDAHSKREVPEYILENKISFYEVKVVRGPLTAAEAGNDSQAQAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.034 kDa

MIIVTNTAKITKGNGHKLIERFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSAAFKDAHSHQGGMPEYILDNKIAYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.034 kDa

MIIVTNTAKITKGNGHKLIERFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSAAFKDAHSHQGGMPEYILDNKIAYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.034 kDa

MIIVTNTAKITKGNGHKLIERFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSAAFKDAHSHQGGMPEYILDNKIAYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.004 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAHSHQGGMPDYILDNKISYYDVKVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.062 kDa

MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKDAHSHQGGMPDYILDNKITYYNVEVVRMPMAAAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.302 kDa

MVIVANKTLIRKGEGHKLVKRFDKIGKIEMQKGFLGLEVLVNAKEKEVDEVTISTRWETKADFHAWTKSEAFREAHSGRNARPDYILGNEIEFYDVEVVRMPIAQAQ

isdG

Heme-degrading monooxygenase

107 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 biliverdin 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.

12.056 kDa

MIIVTNTTKITKGNGHKLIERFNKVGKVETMSGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSSAFKDAHSHQGGMPDYILDNKIAYYDVKVVRMPMAAAQ

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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 staphylobilins (a mixture of 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing) 1

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing)

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing)

107 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.

12.546 kDa

MKFMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRSKNEDESSPIINNKVITYDIGYSYMK

isdG

Heme oxygenase (staphylobilin-producing)

104 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.

12.023 kDa

MFVVTNRITVKKGYAKQMAPNFTKGGPIESLKGFEGIEVWQIDKDDYSEDMYVNSWWETEEDFKNWVNSDVFKQAHKNTGKSEDSPVIKSEIVKSNVLSSLNRR

isdG

Heme oxygenase (staphylobilin-producing)

104 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.

12.023 kDa

MFVVTNRITVKKGYAKQMAPNFTKGGPIESLKGFEGIEVWQIDKDDYSEDMYVNSWWETEEDFKNWVNSDVFKQAHKNTGKSEDSPVIKSEIVKSNVLSSLNRR

isdG

Heme oxygenase (staphylobilin-producing)

104 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.

12.025 kDa

MFVVTNRITVKKGFAEKMAPRFTKGGKIEALQGFHKIEVWKVTRDHENEDMYVNTWWETEKDFEAWTKSDAFKEAHQNRDKTSSESSPVISSEIVKATVLSTLN

isdG

Heme oxygenase (staphylobilin-producing)

104 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.

11.938 kDa

MYVVTNRIDVKKGFAEKMAPKFTQGGKIQELEGFQKVEVWLIDDEADYDQMYINTWWDSEDDFKGWLKSDAFKEAHEGKSKTKSDDSPILGNKVVKANVISELS