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entD

Gene
entD
Protein
Enterobactin synthase component D
Organism
Salmonella typhi
Length
234 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
25.739 kDa
Sequence
MLTSHFPLPFAGHRLHIVDFDASSFHEHDLLWLPHHDRLRSAGRKRKAEHLAGRIAAVHALREVGVRAVPGIGDKRQPLWPDGLFGSISHCASTALAVISRQRVGVDIEKIMSQHTATELAPSIIDSDERQILQASSLPFPLALTLAFSAKESVYKAFSDRVTLPGFDSAKITSLNATHISLHLLPAFAAMMAERTVRTEWFQRGNSVITLVSAITRFPHDRSAPASILSAIPR

Gene
entD
Protein
Enterobactin synthase component D
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
234 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
25.826 kDa
Sequence
MLTSHFPLPFAGHRLHIVDFDASSFREHDLLWLPHHDRLRSAGRKRKAEHLAGRIAAVHALREVGVRTVPGMGDKRQPLWPDGLFGSISHCATTALAVISRQRIGIDIEKIMSQHTATELAPSIIDSDERQILQASLLPFPLALTLAFSAKESVYKAFSDRVTLPGFNSAKVTSLTATHISLHLLPAFAATMAERTVRTEWFQRDNSVITLVSAITRVPHDRSAPASILSAIPR

Gene
entD
Protein
Enterobactin synthase component D
Organism
Salmonella austin
Length
232 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
25.556 kDa
Sequence
MLTSHFPLSFAGHRLHIVDFDASSFHEHDLLWLPHHDRLRSAGRKRKAEHLAGRIAAVHALRRWASGVPGIGDKRQPLWPDDLFGSISHCASTALAVISRQRVGVDIEKIMSQHTATELAVIIDSDEPQILQASSLPFPLALTLAFSAKESVYKAFSDRVSLPGFDSAKVTSLTATHISLHLLPAFAATMAERTVRTEWFQRGNSVITLVSALTRWPHDRSAPASILSAIPR

Gene
entD
Protein
Enterobactin synthase component D
Organism
Escherichia coli O157:H7
Length
206 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
23.131 kDa
Sequence
MKTTHTSLPFAGHTLHFVEFDPANFCEQDLLWLPHYAQLQHAGRKRKTEHLAGRIAAVYALREYGYKCVPAIGELRQPVWPAEVYGSISHCGATALAVVSRQPIGVDIEEIFSAQTATELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD

Gene
entD
Protein
Enterobactin synthase component D
Organism
Escherichia coli (strain K12)
Length
206 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
23.259 kDa
Sequence
MKTTHTSLPFAGHTLHFVEFDPANFCEQDLLWLPHYAQLQHAGRKRKTEHLAGRIAAVYALREYGYKCVPAIGELRQPVWPAEVYGSISHCGTTALAVVSRQPIGIDIEEIFSVQTARELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD

Gene
entD
Protein
Enterobactin synthase component D
Organism
Shigella flexneri
Length
206 amino acids
Function
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Similarity
Belongs to the P-Pant transferase superfamily. EntD family.
Mass
23.131 kDa
Sequence
MKTTHTSLPFAGHTLHFVEFDPANFCEQDLLWLPHYAQLQHAGRKRKTEHLAGRIAAVYALREYGYKCVPAIGELRQPVWPAEVYGSISHCGATALAVVSRQPIGVDIEEIFSAQTATELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD