Exact emitted record, retrieved 2026-09-10T14:34:42.354362+00:00.
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis
PLI (CS 0; PARALOG_OVERANNOTATION). The donor is a bacterial FabG beta-ketoacyl-ACP reductase. Q567K5 instead has the full-length DCXR-like sequence and conserved catalytic architecture supporting soluble L-xylulose/carbonyl reduction. Related NADPH-dependent SDR chemistry does not establish ACP recognition or membership in fatty-acid-chain elongation. This is not a claim that animals lack all ACP-dependent fatty-acid synthesis; it is a distinction between the two enzyme branches. PMID:11882650(https://pubmed.ncbi.nlm.nih.gov/11882650/); sequence comparison; donor.
The assessment concerns the selected accession Q567K5. Other emitted outputs and evidence context.