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Fig. 1 | BMC Evolutionary Biology

Fig. 1

From: Insights into the evolution of enzyme substrate promiscuity after the discovery of (βα)8 isomerase evolutionary intermediates from a diverse metagenome

Fig. 1

Enzymatic activities of the HisA / PriA enzyme superfamily. HisA is a ubiquitous enzyme that catalyzes the conversion of N’-[(5′-phosphoribosyl) formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (ProFAR) into N’-[(5′-phosphoribulosyl) formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR). PriA, exclusively found in the Actinobacteridae class of the high G + C Gram positive bacteria, evolved from HisA to catalyze, in addition to the HisA activity, the conversion of phosphoribosyl anthranilate (PRA) into 1-[(2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate (CdRP). This latter activity is the same as that catalyzed by the ubiquitous TrpF enzyme. subHisA has recently evolved from PriA (indicated with a gray arrow), and it is found exclusively in certain, but not all, Corynebacterium species. As with HisA, subHisA is mono-functional enzyme

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BMC Ecology and Evolution

ISSN: 2730-7182

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