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InterPro: IPR015890 Chorismate binding, C-terminal
Protein matches
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UniProtKB Matches: 4405 proteins |
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Accession
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IPR015890 Chorismate-bd_C |
Secondary
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IPR000350
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IPR005801
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Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR004561 Isochorismate synthase
IPR005256 Anthranilate synthase component I
IPR005257 Anthranilate synthase component I, TrpE
IPR005801 ADC synthase
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
IPR019996 Salicylate synthase
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Contains
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IPR019999 Anthranilate synthase component I, C-terminal
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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 the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.
Anthranilate synthase catalyses the reaction:
chorismate + l-glutamine = anthranilate + pyruvate + l-glutamate.
The enzyme is a tetramer comprising 2 I and 2 II components: this entry is restricted to component I that
catalyses the formation of anthranilate using ammonia rather than glutamine, while component II
provides glutamine amidotransferase activity IPR006220.
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Structural links
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Database links
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Additional Reading
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Parsons JF, Shi KM, Ladner JE.
Structure of isochorismate synthase in complex with magnesium.
Acta Crystallogr. D Biol. Crystallogr. 64 2008 607-10
[PubMed: 18453696]
http://dx.doi.org/10.1107/S0907444908005477
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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 2006 524-34
[PubMed: 16434053]
http://dx.doi.org/10.1016/j.jmb.2005.12.078
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Dosselaere F, Vanderleyden J.
A metabolic node in action: chorismate-utilizing enzymes in microorganisms.
Crit. Rev. Microbiol. 27 2001 75-131
[PubMed: 11450855]
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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 2006 6081-91
[PubMed: 16923875]
http://dx.doi.org/10.1128/JB.00338-06
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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 2001 6021-6
[PubMed: 11371633]
http://dx.doi.org/10.1073/pnas.111150298
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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 2002 2198-208
[PubMed: 11841211]
http://dx.doi.org/10.1021/bi015791b
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Zwahlen J, Kolappan S, Zhou R, Kisker C, Tonge PJ.
Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis.
Biochemistry 46 2007 954-64
[PubMed: 17240979]
http://dx.doi.org/10.1021/bi060852x
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InterPro 23.1
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