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InterPro: IPR015890 Chorismate binding, C-terminal

Protein matchesHelp
UniProtKB
Matches:
4405 proteins
AccessionHelp IPR015890 Chorismate-bd_C
SecondaryHelp IPR000350 , IPR005801
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in 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
Contains IPR019999 Anthranilate synthase component I, C-terminal
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
SCOP: d.161.1.1
CATH: 3.60.120.10
Database linksHelp
PANDIT: PF00425

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR015890 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00897 Anthranilate synthase component 1

P00899 Anthranilate synthase component 1

P20170 Probable anthranilate synthase component 1

P32068 Anthranilate synthase component I-1, chloroplastic

Q06128 Anthranilate synthase component 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR019999 Anthranilate synthase component I, C-terminal
IPR010116 Anthranilate synthase component I, archaeal
IPR006805 Anthranilate synthase component I, N-terminal
IPR005801 ADC synthase
IPR015890 Chorismate binding, C-terminal
IPR005256 Anthranilate synthase component I
IPR005257 Anthranilate synthase component I, TrpE
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
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
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
Dosselaere F, Vanderleyden J.
A metabolic node in action: chorismate-utilizing enzymes in microorganisms.
Crit. Rev. Microbiol. 27 2001 75-131 [PubMed: 11450855]
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
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
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
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