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SDR family oxidoreductase
This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included. [1]. 9351246. The Arabidopsis MALE STERILITY 2 protein shares similarity with reductases in elongation/condensation complexes. Aarts MG, Hodge R, Kalantidis K, Florack D, Wilson ZA, Mulligan BJ, Stiekema WJ, Scott R, Pereira A;. Plant J 1997;12:615-623. (from Pfam)
NAD-dependent epimerase/dehydratase family protein
This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. [1]. 9174344. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM;. Biochemistry 1997;36:6294-6304. (from Pfam)
phosphopantetheine-binding protein
A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. (from Pfam)
AMP-binding protein
carboxylic acid reductase
AFD_CAR-like and SDR_e1 domain-containing protein
thioester reductase domain-containing protein
This model describes a thioester reductase domain that occurs invariably at the C-terminus of proteins that contain it. Most proteins with the domain are non-ribosomal peptide synthetases (NRPS), but the domain also occurs in some polyketide synthases (PKS). The domain participates in biosynthetic pathways in which substrate is activated by adenylation, then transferred as a thioester to a protein's covalently linked pantetheine cofactor. The thioester bond is then reduced, breaking the bond to release the product, and to regenerate the pantetheine thiol (PMID:11254122). Examples of this domain include the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine (PMID:10320345), as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG (PMID:11029592). The activity of this domain is fundamentally different from the more common beta-ketoreductase domains of PKS, which act at a carbonyl two carbons removed from the thioester and form an alcohol as a product.
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