EC Number   |
General Information |
Reference |
|---|
   7.6.2.8 | more |
ABC importers follow the two-site access model3, in which ATP binding and hydrolysis switch the accessibility of the transmembrane domain for the substrate from an inward facing (accessible from the cytoplasm) to an outward-facing (accessible from the extracellular site) conformation, conformational changes by single-molecule FRET measurements combined with molecular dynamics simulations, two different transport cycles are analyzed |
751644 |
| 7.6.2.8 | malfunction |
ABCD4 dysfunction results in a failure of lysosomal vitamin B12 release |
749821 |
| 7.6.2.8 | physiological function |
ABCD4 is a transporter of cobalamin and forms a complex with LMBD1 for the proper targeting or functioning, or both. The two proteins function as a complex |
752200 |
| 7.6.2.8 | physiological function |
ABCD4 is located on lysosomal membrane and is involved in the transport of vitamin B12 from lysosomes to the cytosol |
749821 |
| 7.6.2.8 | physiological function |
ATP-binding cassette (ABC) transporters are a large family of integral membrane proteins and involved in nutrient uptake, drug extrusion, and lipid homeostasis. They use the energy of ATP binding and hydrolysis to power substrate transport across the lipid bilayer. BtuCD-F is an ABC transporter that mediates cobalamin (Cbl) uptake into Escherichia coli, Escherichia coli is unable to synthesize Cbl de novo. BtuCD-F might also be involved in the uptake of cobinamide, a cobalamin precursor. Precursor cobinamide (Cbi) lacks the 5,6-dimethylbenzimidazole (DMB) moiety and sugar-phosphate linker and is therefore smaller than Cbl. BtuCD-catalyzed in vitro transport of cyano-cobinamide is ATP- and BtuF-dependent. BtuF residue W66 is important for high affinity Cbi binding, but not for substrate delivery or transport |
752221 |
| 7.6.2.8 | physiological function |
ATP-binding cassette (ABC) transporters form the largest class of active membrane transport proteins. Binding and hydrolysis of ATP by their highly conserved nucleotide-binding domains drive conformational changes of the complex that mediate transport of substrate across the membrane. The transporter complex of vitamin B12 importer BtuCD-F from Escherichia coli is consisting of a periplasmic soluble binding protein BtuF that binds the ligand and the transmembrane and ATPase domains BtuCD mediating translocation |
751661 |
| 7.6.2.8 | physiological function |
bacterial ABC importers catalyze the uptake of essential nutrients including transition metals and metal-containing cofactors |
752215 |
| 7.6.2.8 | physiological function |
cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii, ECF-CbrT, mediates the specific, ATP-dependent uptake of cobalamin. Cobalamin (vitamin B12) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Enzyme ECF-CbrT catalyzes ATP-dependent transport of cobalamin and cobinamide |
-, 750412 |
| 7.6.2.8 | more |
conformational coupling, molecular dynamics simulations using BtuCD-F is embedded in a solvated phosphatidylcholine bilayer, configurational entropy, pairwise residue-residue forces in BtuCD-F are analyzed through force distribution analysis, overview |
750063 |
| 7.6.2.8 | evolution |
ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family |
-, 750412 |
