Protein Information

General Information
MoonProt ID5
First appeared in release1.0
Name(s)1-Cys peroxiredoxin 1-Cys PRX Peroxiredoxin-6 Human Prx enzyme Non-selenium Glutathione peroxidase Acidic calcium-independent phospholipase A2 aiPLA2
UniProt IDP30041 (PRDX6_HUMAN), Reviewed
GO termsGO: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 GO:0004602 glutathione peroxidase activity
Organisms for which functions have been demonstratedHomo sapiens
Sequence length224
FASTA sequence>sp|P30041|PRDX6_HUMAN Peroxiredoxin-6 OS=Homo sapiens GN=PRDX6 PE=1 SV=3 MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVDWKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
Structure Information
PDB ID1PRX
Quaternary structure
Function 1
Function descriptionAcidic calcium-independent Phospholipase A2 (aiPLA2): regulation of phospholipid turnover
References for functionChen 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.
E.C. number3.1.1.4
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 Active site:140,47 Other functional site:32
Cellular location of functionlysosomes and lung secretory organelles
Comments
Function 2
Function descriptionNon-selenium Glutathione Peroxidase Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides
References for functionChen 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. number1.11.1.15
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 functionlysosome
CommentsThe 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.