SLC25A38 is a mitochondrial inner membrane transporter that plays a critical role in erythropoiesis and cellular metabolism. Its primary function is to facilitate mitochondrial pyridoxal 5'-phosphate (PLP, the active form of vitamin B6) accumulation 1, and it serves as a glycine transporter required for heme biosynthesis initiation 2. SLC25A38 loss causes selective depletion of mitochondrial PLP, impairing PLP-dependent enzymatic reactions including serine hydroxymethyltransferase-2 and ornithine aminotransferase, which disrupts one-carbon unit production and nucleotide synthesis 1. The protein also co-localizes with purinosomes near mitochondrial membranes to facilitate glycine uptake for purine biosynthesis 3. Mutations in SLC25A38 cause congenital sideroblastic anemia type 2 (CSA2), the most common recessive form of this inherited disorder 4. SLC25A38-associated CSA is characterized by reduced heme content, impaired mitochondrial respiration, increased mitochondrial iron, and elevated oxidative stress 5. The disease shows extreme hypersensitivity to pyridoxine deficiency 6. P2 receptor antagonists and combination therapy with glycine plus folate show promise in rescuing heme deficiency in cellular models 52. Additionally, SLC25A38 downregulation is associated with increased metastatic risk and poor prognosis in uveal melanoma 7, and genetic variation in SLC25A38 correlates with dentate gyrus volume in schizophrenia 8.