Os04g0473900
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Contents
Annotated Information
Function
This gene is regarded as DWA1.Putative DWA1 plays important roles in drought resistance.The DWA1 is composed of seven exons(Fig.1) The open reading fame (7,176 bp) encodes a protein consisting of 2,391 aa in japonica rice, Nipponbare, which is one of the 30 megaproteins (>2,300 aa) predicted in the rice genome[1].DWA1,likely to a megaenzyme,has five domains at least. The N terminus of DWA1 is an oxidoreductase-like domain,and closely followed by the AMP-binding domain(A domain)Then,two repeats of a phosphopantetheine-binding subdomain follow the A domain and feature a thiolation domain (T domain).An allene oxide synthase (AOS)-like domain is located between the second and third repeats of the left-handed β-helix (LbH) domain at the C-terminal region[1].
Expression
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Evolution
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At present,homologous sequences with DWA1are all from microorganisms.Nonribosomal peptide synthetase(NRPS),a megaenzyme needed for nonribosomal peptides synthesis in bacteria and filamentous fungi[2],is a major branch of the AMP-binding enzyme superfamily.More importantly,both these homologous sequences and DWA1have an NRPS module, including adenylation domain, followed by a thiolation domain catalyzing the activation and thiolation reaction of an amino acid instead of a carboxyl substrate for acyl-CoA synthetase.These features suggest that DWA1 and its plant homologs may be derived from a prokaryotic NRPS rather than the acyl-CoA synthetase family, which possesses only the A domain[1].
Labs working on this gene
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References
<references> [1]
[2]- ↑ 1.0 1.1 1.2 1.3 1.4 Xiaoyi Zhu, Lizhong Xiong.（2013）Putative megaenzyme DWA1 plays essential roles in drought resistance by regulating stress-induced wax deposition in rice.PANS 110(44): 17790-17795.
- ↑ 2.0 2.1 Marahiel MA, Stachelhaus T, Mootz HD.(1997) Modular peptide synthetases involved in nonribosomal peptide synthesis.Chem Rev 97(7):2651–2674.
