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InterPro: IPR005257 Anthranilate synthase component I, TrpE

Protein matchesHelp
UniProtKB
Matches:
326 proteins
AccessionHelp IPR005257 TrpE_synth
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR005801 ADC synthase
IPR006805 Anthranilate synthase component I, N-terminal
IPR015890 Chorismate binding, C-terminal
IPR019999 Anthranilate synthase component I, C-terminal
GO Term annotationHelp
Process GO:0009058 biosynthetic process
Function GO:0004049 anthranilate synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family represents anthranilate/para-aminobenzoate synthase component I from proteobacteria and actinobacteria.

This enzyme resembles some other chorismate-binding enzymes, including para-aminobenzoate synthase (pabB) and isochorismate synthase. There is a fairly deep split between two sets, seen in the pattern of gaps as well as in amino acid sequence differences. This group includes proteobacteria such as Escherichia coli and Helicobacter pylori (Campylobacter pylori) but also the Gram-positive organism Corynebacterium glutamicum. The second group (IPR005256) includes eukaryotes, archaea, and most other bacterial lineages; sequences from the second group may resemble pabB more closely than other trpE from this group.

Structural linksHelp
SCOP: d.161.1.1
CATH: 3.60.120.10
Database linksHelp
Enzyme: EC:4.1.3.27

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005257 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00897 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
IPR006805 Anthranilate synthase component I, N-terminal
IPR005801 ADC synthase
IPR015890 Chorismate binding, C-terminal
IPR005257 Anthranilate synthase component I, TrpE
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Morollo AA, Eck MJ.
Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
Nat. Struct. Biol. 8 2001 243-7 [PubMed: 11224570]
http://dx.doi.org/10.1038/84988
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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InterPro 23.1