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InterPro: IPR006805 Anthranilate synthase component I, N-terminal

Protein matchesHelp
UniProtKB
Matches:
2443 proteins
AccessionHelp IPR006805 Anth_synth_I_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in 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
GO Term annotationHelp
Process GO:0009058 biosynthetic process
Function GO:0016833 oxo-acid-lyase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Anthranilate synthase catalyses the first step in the biosynthesis of tryptophan. Component I catalyses the formation of anthranilate using ammonia and chorismate. The catalytic site lies in the adjacent region, described in the chorismate binding enzyme family (IPR005801). This region is involved in feedback inhibition by tryptophan [1]. This family also contains a region of Para-aminobenzoate synthase component I.

Structural linksHelp
SCOP: d.161.1.1
CATH: 3.60.120.10
Database linksHelp
Enzyme: EC:4.1.3.27
PANDIT: PF04715
Blocks: IPB006805

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006805 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
1. 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

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
Knochel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN.
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Proc. Natl. Acad. Sci. U.S.A. 96 1999 9479-84 [PubMed: 10449718]
http://dx.doi.org/10.1073/pnas.96.17.9479
Dosselaere F, Vanderleyden J.
A metabolic node in action: chorismate-utilizing enzymes in microorganisms.
Crit. Rev. Microbiol. 27 2001 75-131 [PubMed: 11450855]
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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InterPro 23.1