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IPR001853 is a DSBA-like thioredoxin domain.
<p>DSBA is a sub-family of the Thioredoxin family [[cite:PUB00003378]]. The efficient and correct folding of bacterial disulphide bonded proteins<i>in vivo</i>is dependent upon a class of periplasmic oxidoreductase proteins called DsbA, after the Escherichia coli enzyme. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyses disulphide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilising active-site interactions in the reduced form. DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulphide at the active site [[cite:PUB00006416]]. In the pathogenic bacterium Vibrio cholerae, the DsbA homologue (TcpG) is responsible for the folding, maturation and secretion of virulence factors. <p>While the overall architecture of TcpG and DsbA is similar and the surface features are retained in TcpG, there are significant differences. For example, the kinked active site helix results from a three-residue loop in DsbA, but is caused by a proline in TcpG (making TcpG more similar to thioredoxin in this respect). Furthermore, the proposed peptide binding groove of TcpG is substantially shortened compared with that of DsbA due to a six-residue deletion. Also, the hydrophobic pocket of TcpG is more shallow and the acidic patch is much less extensive than that of E. coli DsbA [[cite:PUB00003378]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Protein disulfide oxidoreductase activity | Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | DSBA-like thioredoxin domain containing protein [Medicago truncatula] gi|357502469|ref|XP_003621523.1| | 9 | ||
| – | DSBA-like thioredoxin domain containing protein [Medicago truncatula] gi|357502473|ref|XP_003621525.1| | 9 | ||
| – | DSBA oxidoreductase family protein; TAIR: AT5G38900.1 Thioredoxin superfamily protein; Swiss-Prot: sp|P39598|YWBO_BACSU Uncharacterized protein YwbO; TrEMBL-Plants: tr|I3S078|I3S078_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0518500 | 8 | ||
| – | DSBA oxidoreductase family protein; TAIR: AT5G38900.1 Thioredoxin superfamily protein; Swiss-Prot: sp|P39598|YWBO_BACSU Uncharacterized protein YwbO; TrEMBL-Plants: tr|I3S078|I3S078_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0518500 | 8 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd03024 | CDD | 1 | 25.00 |