formate/nitrite transporter (FNT) family protein is permeable to formate and nitrate ions as well as hydrosulphide ions, similar to Escherichia coli inner membrane protein YfdC
Formate/nitrite transporter; Proteins in this entry belong to the Formate-Nitrite Transporter ...
9-249
8.57e-73
Formate/nitrite transporter; Proteins in this entry belong to the Formate-Nitrite Transporter (FNT) family and includes the nitrite transport protein NirC and formate channel FocA. They have a pentameric architecture with structural similarity to aquaporins and glyceroporins. Proteins in this family transport the structurally related compounds, formate and nitrite.
Pssm-ID: 460122 Cd Length: 244 Bit Score: 223.14 E-value: 8.57e-73
formate/nitrite transporter; The Formate-Nitrite Transporter (FNT) Family (TC 2.A.44)The ...
20-253
2.24e-51
formate/nitrite transporter; The Formate-Nitrite Transporter (FNT) Family (TC 2.A.44)The prokaryotic proteins of the FNT family probably function in the transport of the structurally related compounds, formate and nitrite. The homologous yeast protein may function as a short chain aliphatic carboxylate H+ symporter,transporting formate, acetate and propionate, and functioning primarily as an acetate uptake permease. The putative formate efflux transporters (FocA) of bacteria associated with pyruvate-formate lyase (pfl) comprise cluster I; the putative formate uptake permeases (FdhC) of bacteria and archaea associated with formate dehydrogenase comprise cluster II; the putative nitrite uptake permeases (NirC) of bacteria comprise cluster III, and the single yeast protein, the putative acetate:H+ symporter alone comprises cluster IV. The energy coupling mechanisms for proteins of the FNT family have not been extensively characterized. HCO2 -, CH3CO2 - and NO2 - uptakes are probably coupled to H+symport. HCO2 - efflux may be driven by the membrane potential by a uniport mechanism or by H+ antiport. [Transport and binding proteins, Anions]
Pssm-ID: 273269 Cd Length: 239 Bit Score: 168.24 E-value: 2.24e-51
Formate/nitrite transporter; Proteins in this entry belong to the Formate-Nitrite Transporter ...
9-249
8.57e-73
Formate/nitrite transporter; Proteins in this entry belong to the Formate-Nitrite Transporter (FNT) family and includes the nitrite transport protein NirC and formate channel FocA. They have a pentameric architecture with structural similarity to aquaporins and glyceroporins. Proteins in this family transport the structurally related compounds, formate and nitrite.
Pssm-ID: 460122 Cd Length: 244 Bit Score: 223.14 E-value: 8.57e-73
formate/nitrite transporter; The Formate-Nitrite Transporter (FNT) Family (TC 2.A.44)The ...
20-253
2.24e-51
formate/nitrite transporter; The Formate-Nitrite Transporter (FNT) Family (TC 2.A.44)The prokaryotic proteins of the FNT family probably function in the transport of the structurally related compounds, formate and nitrite. The homologous yeast protein may function as a short chain aliphatic carboxylate H+ symporter,transporting formate, acetate and propionate, and functioning primarily as an acetate uptake permease. The putative formate efflux transporters (FocA) of bacteria associated with pyruvate-formate lyase (pfl) comprise cluster I; the putative formate uptake permeases (FdhC) of bacteria and archaea associated with formate dehydrogenase comprise cluster II; the putative nitrite uptake permeases (NirC) of bacteria comprise cluster III, and the single yeast protein, the putative acetate:H+ symporter alone comprises cluster IV. The energy coupling mechanisms for proteins of the FNT family have not been extensively characterized. HCO2 -, CH3CO2 - and NO2 - uptakes are probably coupled to H+symport. HCO2 - efflux may be driven by the membrane potential by a uniport mechanism or by H+ antiport. [Transport and binding proteins, Anions]
Pssm-ID: 273269 Cd Length: 239 Bit Score: 168.24 E-value: 2.24e-51
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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