FEBS Lett.

Based on the functional characterization of sucrose biosynthesis related protiens[SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species and plants, and that they are multidomain proteins with modular architecture. Anabaena SPS, a minimal catalytic SPS unit, defines a glucosyltransferase domain present in all SPSs and SuSs. Similarly, Anabaena SPP defines a phosphohydrolase domain characteristic of all SPPs and some SPSs. Phylogenetic analysis points towards the evolution of modern cyanobacterial and plant SBP from a bidomainal common ancestral SPS-like gene.

Source:http://purl.uniprot.org/citations/12062401

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http://purl.uniprot.org/cit...rdfs:commentBased on the functional characterization of sucrose biosynthesis related protiens[SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species and plants, and that they are multidomain proteins with modular architecture. Anabaena SPS, a minimal catalytic SPS unit, defines a glucosyltransferase domain present in all SPSs and SuSs. Similarly, Anabaena SPP defines a phosphohydrolase domain characteristic of all SPPs and some SPSs. Phylogenetic analysis points towards the evolution of modern cyanobacterial and plant SBP from a bidomainal common ancestral SPS-like gene.lld:uniprot
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http://purl.uniprot.org/cit...uniprot:authorCumino A.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorSalerno G.L.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorCuratti L.lld:uniprot
http://purl.uniprot.org/cit...uniprot:authorGiarrocco L.lld:uniprot
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http://purl.uniprot.org/cit...uniprot:titleSucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution.lld:uniprot
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