| General Information |
| MoonProt ID | 437 |
| First appeared in release | 3.0 |
| Name(s) | 2-cys peroxiredoxin, Prx, Prx1, gene: Smp_059480 |
| UniProt ID | G4VKD9 |
| GO terms | GO:0055114 oxidation-reduction process
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0051920 peroxiredoxin activity
GO:0004601 peroxidase activity
GO:0098869 cellular oxidant detoxification |
| Organisms for which functions have been demonstrated | Schistosoma mansoni(Blood fluke), human parasite |
| Sequence length | 185 amino acids |
| FASTA sequence | >tr|G4VKD9|G4VKD9_SCHMA Peroxiredoxin, Prx1 OS=Schistosoma mansoni OX=6183 GN=Smp_059480 PE=4 SV=1
MVLLPNRPAPEFKGQAVINGEFKEICLKDYRGKYVVLFFYPSDFTFVCPTEIIAFSDQVEEFNSRNCQVIACSTDSQYSHLAWDNLDRKSGGLGHMKIPLLADRKQEISKAYGVFDEEDGNAFRGLFIIDPNGILRQITINDKPVGRSVDETLRLLDAFQFVEKHGEVCPVNWKRGQHGIKVNQK |
| Structure Information |
| PDB ID | 3ZVJ, 3ZTL, 3ZL5, 3ZLP |
| Quaternary structure | Decameric ring assembly for SmPrxI-LMW and a double decamer for SmPrxl-HMWr |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
moonID_437_uniID_G4VKD9 is 185 residues long, with 10 residues (5.41%) predicted as disordered.The protein has 1 short (< 30 residues) disorder segment and 0 long (>= 30 residues) disorder segments.
Segment 1 - Short (< 30 residues) disordered segment Segment is located between positions 176 and 185 in the sequence. The segment is 10 residues long (5.41 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | peroxidase (Sm-Prxl-LMW), thioredoxin-dependent peroxidase in the absence of oxidative stress, uses redox-active cysteine to reduce H2O2 |
| References for function | Saccoccia F, Di Micco P, Boumis G, Brunori M, Koutris I, Miele AE, Morea V, Sriratana P, Williams DL, Bellelli A, Angelucci F. Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin. Structure. 2012 20(3):429-39. doi: 10.1016/j.str.2012.01.004. PMID: 22405002; PMCID: PMC3299984. |
| E.C. number | 1.11.1.15 |
| Location of functional site(s) | Cysteine sulfenic acid (-SOH) intermediate; active sites are in the fully folded (FF) conformation in the first turn of the alpha 2 helix and beta 3 - alpha 2 loop |
| Cellular location of function | mitochondria |
| Comments | LMW decamer |
| Function 2 |
| Function description | chaperone, ATP-independent holdases at high hydrogen peroxide concentrations, prevent protein aggregation by quarantining client proteins |
| References for function | Saccoccia F, Di Micco P, Boumis G, Brunori M, Koutris I, Miele AE, Morea V, Sriratana P, Williams DL, Bellelli A, Angelucci F. Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin. Structure. 2012 20(3):429-39. doi: 10.1016/j.str.2012.01.004. PMID: 22405002; PMCID: PMC3299984. |
| E.C. number | NA |
| Location of functional site(s) | NA |
| Cellular location of function | cytoplasm |
| Comments | Has a weak presence at pH 4.2 under reducing conditions, active when overoxidized SmPrxI-SO2H/SO3H is at pH 7, HMW 20-mer formed by two stacked decamers |