| Symbol: | Form_Nir_trans |
| Form_Nir_trans | |
| Pfam: | PF01226 |
| Interpro: | IPR000292 |
| Prosite: | PDOC00769 |
| Tcdb: | 2.A.44 |
| Opm Family: | 7 |
| Opm Protein: | 3tdp |
The Formate-Nitrite Transporter (FNT) Family belongs to the Major Intrinsic Protein (MIP) Superfamily.[1] [2] FNT family members have been sequenced from Gram-negative and Gram-positive bacteria, archaea, yeast, plants and lower eukaryotes. The prokaryotic proteins of the FNT family probably function in the transport of the structurally related compounds, formate and nitrite.[3]
With the exception of the yeast protein (627 amino acyl residues), all characterized members of the family are of 256-285 residues in length and exhibit 6-8 putative transmembrane α-helical spanners (TMSs). In one case, that of the E. coli FocA (TC# 1.A.16.1.1) protein, a 6 TMS topology has been established.[4] The yeast protein has a similar apparent topology but has a large C-terminal hydrophilic extension of about 400 residues.
FocA of E. coli is a symmetric pentamer, with each subunit consisting of six TMSs.
The phylogenetic tree shows clustering according to function and organismal phylogeny. The putative formate efflux transporters (FocA; TC#s 1.A.16.1.1 and 1.A.16.1.3) of bacteria associated with pyruvate-formate lyase (pfl) comprise cluster I; the putative formate uptake permeases (FdhC; TC#s 1.A.16.2.1 and 1.A.16.2.3) of bacteria and archaea associated with formate dehydrogenase comprise cluster II; the nitrite uptake permeases (NirC, TC#s 1.A.16.2.5, 1.A.16.3.1, and 1.A.16.3.4) of bacteria comprise cluster III, and a yeast protein comprises cluster IV.[5]
The energy coupling mechanisms for proteins of the FNT family have not been extensively characterized. HCO and NO uptakes may be coupled to H+ symport. HCO efflux may be driven by the membrane potential by a uniport mechanism or by H+ antiport. FocA of E. coli catalyzes bidirectional formate transport and may function by a channel-type mechanism.[6]
FocA, transports short-chain acids. FocA may be able to switch its mode of operation from a passive export channel at high external pH to a secondary active formate/H+ importer at low pH. The crystal structure of Salmonella typhimurium FocA at pH 4.0 shows that this switch involves a major rearrangement of the amino termini of individual protomers in the pentameric channel.[7] The amino-terminal helices open or block transport in a concerted, cooperative action that indicates how FocA is gated in a pH-dependent way. Electrophysiological studies show that the protein acts as a specific formate channel at pH 7.0 and that it closes upon a shift of pH to 5.1.
The probable transport reactions catalyzed by different members of the FNT family are:
(1) RCO or NO (out) ⇌ RCO or NO (in),
(2) HCO (in) ⇌ HCO (out),
(3) HS− (out) ⇌ HS− (in).
A representative list of the currently classified members belonging to the FNT family can be found in the Transporter Classification Database. Some characterized members include: