From Wikipedia, the free encyclopedia
Thia_YuaJ
Identifiers
SymbolThia_YuaJ
Pfam PF09515
Pfam clan CL0315
InterPro IPR012651
OPM superfamily 134
OPM protein 3rlb
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Members of this protein family have been assigned as thiamine transporters by a phylogenomic analysis of families of genes regulated by the THI element, a broadly conserved RNA secondary structure element through which thiamine pyrophosphate (TPP) levels can regulate transcription of many genes related to thiamine transport, salvage, and de novo biosynthesis. Species with this protein always lack the ThiBPQ ABC transporter. In some species (e.g. Streptococcus mutans and Streptococcus pyogenes), yuaJ is the only THI-regulated gene. Evidence from Bacillus cereus indicates thiamine uptake is coupled to proton translocation. [1] [2]

This family includes human solute transporters SLC19A1, SLC19A2 and SLC19A3.

References

  1. ^ Erkens GB, Slotboom DJ (April 2010). "Biochemical characterization of ThiT from Lactococcus lactis: a thiamin transporter with picomolar substrate binding affinity". Biochemistry. 49 (14): 3203–12. doi: 10.1021/bi100154r. PMID  20218726.
  2. ^ Eitinger T, Rodionov DA, Grote M, Schneider E (January 2011). "Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions". FEMS Microbiology Reviews. 35 (1): 3–67. doi: 10.1111/j.1574-6976.2010.00230.x. PMID  20497229.
This article incorporates text from the public domain Pfam and InterPro: IPR012651
From Wikipedia, the free encyclopedia
Thia_YuaJ
Identifiers
SymbolThia_YuaJ
Pfam PF09515
Pfam clan CL0315
InterPro IPR012651
OPM superfamily 134
OPM protein 3rlb
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Members of this protein family have been assigned as thiamine transporters by a phylogenomic analysis of families of genes regulated by the THI element, a broadly conserved RNA secondary structure element through which thiamine pyrophosphate (TPP) levels can regulate transcription of many genes related to thiamine transport, salvage, and de novo biosynthesis. Species with this protein always lack the ThiBPQ ABC transporter. In some species (e.g. Streptococcus mutans and Streptococcus pyogenes), yuaJ is the only THI-regulated gene. Evidence from Bacillus cereus indicates thiamine uptake is coupled to proton translocation. [1] [2]

This family includes human solute transporters SLC19A1, SLC19A2 and SLC19A3.

References

  1. ^ Erkens GB, Slotboom DJ (April 2010). "Biochemical characterization of ThiT from Lactococcus lactis: a thiamin transporter with picomolar substrate binding affinity". Biochemistry. 49 (14): 3203–12. doi: 10.1021/bi100154r. PMID  20218726.
  2. ^ Eitinger T, Rodionov DA, Grote M, Schneider E (January 2011). "Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions". FEMS Microbiology Reviews. 35 (1): 3–67. doi: 10.1111/j.1574-6976.2010.00230.x. PMID  20497229.
This article incorporates text from the public domain Pfam and InterPro: IPR012651

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