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
Organisms for which functions have been demonstratedHomo sapiens (human, a mammal, OMIM number 602316 )
Sequence length224
Structure Information
Quaternary structure
SCOPThioredoxin fold
CATH3.40.30.10, 3.30.1020.10
TM Helix Predictionno TM helices
DisProt AnnotationNot in DisProt
Predicted Disorder Regions1-3,224
Connections to Disease
Function 1
Function descriptionAcidic calcium-independent Phospholipase A2 (aiPLA2): regulation of phospholipid turnover
References for functionPMID: 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
Cellular location of functionlysosomes and lung secretory organelles
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.