TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
2.A.46.1.1









Benzoate permease, BenE of 394 aas and 11 - 13 TMSs (Neidle et al. 1991).

Bacteria
Pseudomonadota
BenE of Acinetobacter calcoaceticus
2.A.46.1.2









BenE homologue of 422 aas.

Bacteria
Actinomycetota
BenE of Rodococcus jostii
2.A.46.1.3









BenE homologue of 393 aas and 12 TMSs.

Bacteria
Actinomycetota
BenE  of Kineococcus radiotolerans
2.A.46.1.4









BenE homologue of 398 aas and 14 TMSs.

Bacteria
Actinomycetota
BenE of Cellvibrio gilvus
2.A.46.1.5









BenE homologue of 398 aas and 14 TMSs

Bacteria
Pseudomonadota
BenE of Pseudomonas putida
2.A.46.1.6









BenE homologue of 516 aas with 7 - 9 TMSs and a long hydrophiliic N-terminal domain.

Bacteria
Actinomycetota
BenE of Frankia sp. Ccl3
2.A.46.1.7









BenE homologue of 410 aas and 13 - 14 TMSs.

Bacteria
Pseudomonadota
BenE of Marinobacter adhaerens
2.A.46.1.8









BenE homologue of 458 aas

Bacteria
Pseudomonadota
BenE of Marinobacter hydrocarbonclasticus
2.A.46.1.9









YdcO (BenE homologue) of 391 aas and 13 putative TMSs.

Bacteria
Pseudomonadota
YdcO of E. coli
2.A.46.1.10









Benzoate uptake porter of 423 aas and 12 TMSs, BenE (Choudhary et al. 2017).

Bacteria
Pseudomonadota
BenE of Pseudomonas putida
2.A.46.1.11









Membrane protein PurT of 471 aas and 14 TMSs.  In mammals, the concentrative uptake of ascorbic acid (vitamin C) by members of the NAT family is driven by the Na+ gradient, while the uptake of nucleobases in bacteria is powered by the H+ gradient. The structure of PurC has been determined at 2.80 Å resolution (Weng et al. 2023). PurTCp forms a homodimer, and each protomer has 14 transmembrane segments folded into a transport domain (core domain) and a scaffold domain (gate domain). A purine base is present in the structure and defines the location of the substrate binding site. Functional studies reveal that PurTCp transports purines but not pyrimidines and that purine binding and transport is dependent on the pH. Mutation of a conserved aspartate residue close to the substrate binding site reveals the critical role of this residue in H+-dependent transport of purines. Comparison of the PurTCp structure with transporters of the same structural fold suggests that rigid-body motions of the substrate-binding domain are central for substrate translocation across the membrane (Weng et al. 2023).

Bacteria
Pseudomonadota
PurT of Colwellia psychrerythraea