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InterPro: IPR005801 ADC synthase
Protein matches
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UniProtKB Matches: 4430 proteins |
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Accession
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IPR005801 ADC_synthase |
Secondary
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IPR000350
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IPR010118
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Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR019996 Salicylate synthase
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Found in
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IPR004561 Isochorismate synthase
IPR005256 Anthranilate synthase component I
IPR005257 Anthranilate synthase component I, TrpE
IPR005802 Para-aminobenzoate synthase, component I
IPR010112 Anthranilate synthase, clad 3
IPR010116 Anthranilate synthase component I, archaeal
IPR010117 Para-aminobenzoate synthase
IPR010118 Para-aminobenzoate synthase/anthranilate synthase, component I
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Contains
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IPR006805 Anthranilate synthase component I, N-terminal
IPR015890 Chorismate binding, C-terminal
IPR019999 Anthranilate synthase component I, C-terminal
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GO Term annotation
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Process
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GO:0009058 biosynthetic process
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This entry represents the catalytic regions of ADC synthases, including:
- Anthranilate synthase aminodeoxyisochorismate synthase/lyase subunit, TrpE, which catalyses the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine [1, 2].
- P-aminobenzoate synthase component I (Aminodeoxychorismate synthase), which catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate, a precursor of p-aminobenzoate and folate in microorganisms [3].
- Menaquinone-specific isochorismate synthase MenF, which catalyses the conversion of chorismate to isochorismate [4].
- Salicylate synthetase Irp9, which is involved in the biosynthesis of the siderophore yersiniabactin in Yersinia enterocolitica [5].
- Salicylate synthase MbtI (Mycobactin synthetase protein I), which is involved in salicylate production [6].
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Structural links
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Database links
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Publications
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1.
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Morollo AA, Eck MJ.
Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
Nat. Struct. Biol. 8 243-7 2001
[PubMed: 11224570]
http://dx.doi.org/10.1038/84988
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2.
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Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE.
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Proc. Natl. Acad. Sci. U.S.A. 98 6021-6 2001
[PubMed: 11371633]
http://dx.doi.org/10.1073/pnas.111150298
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3.
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Parsons JF, Jensen PY, Pachikara AS, Howard AJ, Eisenstein E, Ladner JE.
Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes.
Biochemistry 41 2198-208 2002
[PubMed: 11841211]
http://dx.doi.org/10.1021/bi015791b
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4.
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Kolappan S, Zwahlen J, Zhou R, Truglio JJ, Tonge PJ, Kisker C.
Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family.
Biochemistry 46 946-53 2007
[PubMed: 17240978]
http://dx.doi.org/10.1021/bi0608515
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5.
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Kerbarh O, Chirgadze DY, Blundell TL, Abell C.
Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate.
J. Mol. Biol. 357 524-34 2006
[PubMed: 16434053]
http://dx.doi.org/10.1016/j.jmb.2005.12.078
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6.
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Harrison AJ, Yu M, Gardenborg T, Middleditch M, Ramsay RJ, Baker EN, Lott JS.
The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase.
J. Bacteriol. 188 6081-91 2006
[PubMed: 16923875]
http://dx.doi.org/10.1128/JB.00338-06
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InterPro 23.1
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