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Comparative Study
. 2003 Mar;4(3):296-300.
doi: 10.1038/sj.embor.embor771.

Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis

Francisco Barona-Gómez  1 , David A Hodgson
Affiliations
Comparative Study

Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis

Francisco Barona-Gómez et al. EMBO Rep. 2003 Mar.

Abstract

We report the occurrence of an isomerase with a putative (betaalpha)(8)-barrel structure involved in both histidine and trypto-phan biosynthesis in Streptomyces coelicolor A3(2) and Mycobacterium tuberculosis HR37Rv. Deletion of a hisA homologue (SCO2050) putatively encoding N'-[(5'-phosphoribosyl)-formimino]-5 amino-imidazole-4-carboxamide ribonucleotide isomerase from the chromosome of S. coelicolor A3(2) generated a double auxotrophic mutant for histidine and tryptophan. The bifunctional gene SCO2050 and its orthologue Rv1603 from M. tuberculosis complemented both hisA and trpF mutants of Escherichia coli. Expression of the E. coli trpF gene in the S. coelicolor mutant only complemented the tryptophan auxo-trophy, and the hisA gene only complemented the histidine auxotrophy. The discovery of this enzyme, which has a broad-substrate specificity, has implications for the evolution of metabolic pathways and may prove to be important for understanding the evolution of the (betaalpha)(8)-barrels.

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Figures

Figure 1
Figure 1
HisA and TrpF catalyse similar reactions. HisA and TrpF catalyse analogous Amadori rearrangements of N′-[(5′-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (ProFAR) and N′-(5′-phosphoribosyl)anthranilate (PRA) into N′-[(5′-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide (PRFAR) and 1-[(2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate (CDRP), respectively. Red 'R's indicate the different side-chains in the two substrates.
Figure 2
Figure 2
Synteny of the his/trp region and sequence similarity of PriA and HisA. (A) Organization of the his/trp cluster of Streptomyces coelicolor (Bentley et al., 2002) and Mycobacterium tuberculosis (Cole et al., 1998). The hisA homologues of S. coelicolor (SCO2050) and M. tuberculosis (Rv1603) are marked with asterisks. Genes involved in histidine (his; black) and tryptophan (trp; grey) biosynthesis are shown. (B) Sequence alignment of the HisA homologues of S. coelicolor (SC–PriA) and Thermotoga maritima (TM–HisA), which show 25% identity. Data from T. maritima (Jürgens et al., 2000; Hennsax et al., 2002) were used to identify the catalytically important residues in SCO2050 (Asp 11, Asp 130 and Thr 166 (asterisks)). The region of SCO2050 replaced in WH101 (this study) lies between Ala 126 and Gly 210 (indicated by arrows).
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