Protein Family Models

Aconitase X (AcnX) is a subfamily of Acn superfamily. It is encoded in the genomes of many archaea, proteobacteria and fungi. Among archaea, the pattern of aconitase X occurrence complements that of aconitase A such that together the two enzymes account for aconitase activity in all archaea [1]. This protein catalyzes the dehydration of cis-3-hydroxy-L-proline to delta1-pyrroline-2-carboxylate [2]. [1]. 14568143. Filling a gap in the central metabolism of archaea: prediction of a novel aconitase by comparative-genomic analysis. Makarova KS, Koonin EV;. FEMS Microbiol Lett. 2003;227:17-23. [2]. 27929065. Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. Watanabe S, Tajima K, Fujii S, Fukumori F, Hara R, Fukuda R, Miyazaki M, Kino K, Watanabe Y;. Sci Rep. 2016;6:38720. (from Pfam)

Date:

2024-10-16

This is a putative aconitase X swivel domain, which has been predicted by comparative genomic analysis. The domain is mainly found in archaeal and proteobacterial proteins. As such, the prediction should be treated with caution [1]. One member of this entry from Aeropyrum pernix which has been annotated as a putative aconitase, has been characterised in vitro and catalyses the dehydration of mevalonate 5-phosphate to form trans-anhydromevalonate 5-phosphate, a previously unknown intermediate [2], being involved in a "modified" mevalonate pathway. [1]. 14568143. Filling a gap in the central metabolism of archaea: prediction of a novel aconitase by comparative-genomic analysis. Makarova KS, Koonin EV;. FEMS Microbiol Lett. 2003;227:17-23. [2]. 30224495. Modified mevalonate pathway of the archaeon Aeropyrum pernix proceeds via trans-anhydromevalonate 5-phosphate. Hayakawa H, Motoyama K, Sobue F, Ito T, Kawaide H, Yoshimura T, Hemmi H;. Proc Natl Acad Sci U S A. 2018;115:10034-10039. (from Pfam)

Date:

2024-10-16

AcnX_swivel and AcnX domain-containing protein

Date:

2017-03-02