| Literature References | 1. ESSAR, D.W., EBERLY, L., HADERO, A. AND CRAWFORD, I.P.
Identification and characterization of genes for a second anthranilate
synthase in Pseudomonas aeruginosa: Interchangeability of the two
anthranilate synthases, and evolutionary implications.
J.BACTERIOL. 172 884-900 (1990).
2. CRAWFORD, I.P. AND EBERLY, L.
Structure and regulation of the anthranilate synthase genes in Pseudomonas
aeruginosa. Sequence of TrpG encoding the glutamine amidotransferase
subunit.
MOL.BIOL.EVOL. 3 436-448 (1986).
3. SATO, S., NAKADA, Y., HON-NAMI, K., YASUI, K. AND SHIRATSUCHI, A.J.
Molecular cloning and the nucleotide sequence of the Clostridium
thermocellum trpE gene.
J.BIOCHEM.(TOKYO) 105 362-366 (1989).
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| Documentation | Anthranilate synthase catalyses the reaction: chorismate + l-glutamine =
anthranilate + pyruvate + l-glutamate. The enzyme is a tetramer comprising
2 I and 2 II components: component I catalyses the formation of
anthranilate using ammonia rather than glutamine, while component II
provides glutamine amidotransferase activity.
ANTSNTHASEI is a 4-element fingerprint that provides a signature for
anthranilate synthase type I components. The fingerprint was derived from
an initial alignment of 5 sequences: the motifs encode conserved regions
towards the C-terminus of the alignment. Four iterations on OWL11.0 were
required to reach convergence, at which point a true set comprising 18
sequences was identified. Three partial matches were also found.
An update on SPTR37_9f identified a true set of 53 sequences, and 7
partial matches.
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