| General Information |
| MoonProt ID | 5 |
| First appeared in release | 1.0 |
| Name(s) | 1-Cys peroxiredoxin
1-Cys PRX
Peroxiredoxin-6
Human Prx enzyme
Non-selenium Glutathione peroxidase
Acidic calcium-independent phospholipase A2
aiPLA2 |
| UniProt ID | P30041 (PRDX6_HUMAN), Reviewed |
| GO terms | GO:0006629 lipid metabolic process
GO:0006979 response to oxidative stress
GO:0008152 metabolic process
GO:0009395 phospholipid catabolic process
GO:0016042 lipid catabolic process
GO:0042744 hydrogen peroxide catabolic process
GO:0055114 oxidation-reduction process
GO:0003824 catalytic activity
GO:0004601 peroxidase activity
GO:0004602 glutathione peroxidase activity
GO:0004623 phospholipase A2 activity
GO:0005515 protein binding
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0016787 hydrolase activity
GO:0051920 peroxiredoxin activity
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005829 cytosol
GO:0016023 cytoplasmic membrane-bounded vesicle
GO:0031410 cytoplasmic vesicle
GO:0070062 extracellular vesicular exosome |
| Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal, OMIM number 602316 ) |
| Sequence length | 224 |
| FASTA sequence | >sp|P30041|PRDX6_HUMAN Peroxiredoxin-6 OS=Homo sapiens GN=PRDX6 PE=1 SV=3
MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVDWKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP |
| Structure Information |
| PDB ID | 1PRX |
| Quaternary structure | |
| SCOP | Thioredoxin fold |
| CATH | 3.40.30.10, 3.30.1020.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-3,224 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Acidic calcium-independent Phospholipase A2 (aiPLA2):
regulation of phospholipid turnover |
| References for function | PMID: 10893423 |
| E.C. number | 3.1.1.4 |
| Location of functional site(s) | Ser(32) in the GDSWG consensus sequence is the active site which provides the catalytic nucleophile for the hydrolase activity |
| Cellular location of function | lysosomes and lung secretory organelles |
| Comments | |
| Function 2 |
| Function description | Non-selenium Glutathione Peroxidase
Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides |
| References for function | Chen JW, Dodia C, Feinstein SI, Jain MK, Fisher AB. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J Biol Chem. 2000 Sep 15;275(37):28421-7. PMID: 10893423
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat Struct Biol. 1998 May. PMID: 9587003. |
| E.C. number | 1.11.1.15 |
| Location of functional site(s) | The active site for peroxidase activity is Cys(47) in the PVCTTE consensus sequence. It exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environme |
| Cellular location of function | lysosome |
| Comments | The protein has two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. |