Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica
The three-dimensional crystal structure of the PrpF protein of Shewanella oneidensis complexed with trans-aconitate: insights into its biological function.
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S. oneidensis PrpF has a DapF-like fold, isomerizes trans-aconitate to cis-aconitate in vitro, and uses Lys73 (with Cys107 nearby) at the active site. It is required only in bacteria that use AcnD. PrpF and Mii share only 39% identity.
The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle.
UniProt entry Q7VZI5
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Records the PrpF-like domain (IPR007400), the PrpF Pfam domain (PF04303), PANTHER PTHR43709:SF2 and the diaminopimelate epimerase-like fold. The recommended name is generated by ProtNLM, and the family similarity note rests on ARBA. Neither is used as evidence here.
Deep research summary for Q7VZI5
Q7VZI5 PTHR43709 comparison, active-site mapping, genomic context and hydropathy
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Q7VZI5 is 36% identical to the three PrpF proteins (which are 78-80% identical to each other, including B. pertussis BP2370) and lacks TIGR02334. It is 35-45% identical to all other characterised SF2 and SF3 members.
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Q7VZI5 conserves the PrpF catalytic Lys/Cys pair (K65, C99). It has arginine at the PrpF K281 carboxylate-binding position.
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BP0922 lies outside the prp cluster (BP2368-BP2371), next to an MmgE/PrpD-family protein (BP0918) and a succinate-semialdehyde dehydrogenase (BP0919).