FMO5
Chr 1flavin containing dimethylaniline monoxygenase 5
Also known as: hBVMO1
The FMO5 protein functions as a Baeyer-Villiger monooxygenase that catalyzes oxygen insertion into carbon-carbon bonds adjacent to carbonyls, converting ketones to esters, and also modulates cholesterol biosynthesis and glucose homeostasis. While other flavin-containing monooxygenases cause trimethylaminuria when mutated, no specific genetic disorders have been definitively associated with FMO5 mutations despite its metabolic functions. The gene shows high tolerance to loss-of-function variants (LOEUF 1.448), suggesting that complete loss of FMO5 function may be well-tolerated in humans.
Disputed — evidence questions this relationship
Population Genetics & Constraint
gnomAD v4 — loss-of-function & missense intolerance
Highly tolerant — LoF variants common in population
Tolerant to missense variation
This gene has evidence for multiple mechanisms of pathogenicity (dominant-negative and gain-of-function). Both the Badonyi & Marsh prediction and the broader genomic evidence point to dominant-negative as the predominant mechanism. Different variants in this gene may act through different mechanisms — interpret in context of the specific variant.
Note: In-silico variant effect predictors (SIFT, PolyPhen, REVEL, CADD) may underestimate pathogenicity of missense variants in genes with GOF or DN mechanisms. Consider functional evidence and clinical context.
Predictions from Badonyi M, Marsh JA. PLoS ONE. 2024;19(8):e0307312.
ClinVar Variant Classifications
0 submitted variants in ClinVar
Protein Context — Lollipop Plot
FMO5 · protein map & ClinVar variants
Showing all ClinVar variants across the protein. Search a specific variant to highlight its position.
3D Protein StructureAlphaFold
External Resources
Links to major genomics databases and tools
Clinical Trials
Active and recruiting trials from ClinicalTrials.gov
No active trials found for this gene.
Search ClinicalTrials.gov →External Resources
Links to major genomics databases and tools