UniProtKB - Q5R7E0 (PRDX6_PONAB)
Protein
Peroxiredoxin-6
Gene
PRDX6
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Functioni
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).By similarity
Miscellaneous
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation mediated by glutathione S-transferase Pi, followed by spontaneous reduction of the enzyme with glutathione.By similarity
Catalytic activityi
- EC:1.11.1.27By similarity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+By similarityEC:3.1.1.4By similarity
- a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoABy similarityEC:2.3.1.23By similarity
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 32 | Important for phospholipase activityBy similarity | 1 | |
Active sitei | 47 | Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activityBy similarity | 1 | |
Active sitei | 140 | For phospholipase activityBy similarity | 1 |
GO - Molecular functioni
- peroxidase activity Source: UniProtKB-KW
- peroxiredoxin activity Source: InterPro
- phospholipase A2 activity Source: UniProtKB-EC
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
GO - Biological processi
- lipid catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Antioxidant, Hydrolase, Multifunctional enzyme, Oxidoreductase, Peroxidase, Transferase |
Biological process | Lipid degradation, Lipid metabolism |
Protein family/group databases
PeroxiBasei | 4422, Ppy1CysPrx |
Names & Taxonomyi
Protein namesi | Recommended name: Peroxiredoxin-6 (EC:1.11.1.27By similarity)Alternative name(s): 1-Cys peroxiredoxin Short name: 1-Cys PRX Glutathione-dependent peroxiredoxinCurated Lysophosphatidylcholine acyltransferase 5By similarity (EC:2.3.1.23By similarity) Short name: LPC acyltransferase 5 Short name: LPCAT-5 Short name: Lyso-PC acyltransferase 5 Non-selenium glutathione peroxidase Short name: NSGPx |
Gene namesi | Name:PRDX6 |
Organismi | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
Taxonomic identifieri | 9601 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Proteomesi |
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PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000256862 | 1 – 224 | Peroxiredoxin-6Add BLAST | 224 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 44 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 63 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 89 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 177 | Phosphothreonine; by MAPKBy similarity | 1 | |
Modified residuei | 209 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 209 | N6-succinyllysine; alternateBy similarity | 1 |
Post-translational modificationi
Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.By similarity
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (By similarity).By similarity
Keywords - PTMi
Acetylation, PhosphoproteinInteractioni
Subunit structurei
Homodimer (By similarity).
Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (By similarity).
Interacts with APEX1.
Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (By similarity).
By similarityProtein-protein interaction databases
STRINGi | 9601.ENSPPYP00000000577 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 169 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 165 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 31 – 40 | Required and sufficient for targeting to lysosomes and lamellar bodiesBy similarity | 10 |
Sequence similaritiesi
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | KOG0854, Eukaryota |
InParanoidi | Q5R7E0 |
OrthoDBi | 1129256at2759 |
Family and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
i Sequence
Sequence statusi: Complete.
Q5R7E0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF
110 120 130 140 150
PIIDDRNREL AILLGMLDPA EKDEKGMPGT ARVVFVFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGRKYLRY TPQP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR860178 mRNA Translation: CAH92320.1 |
RefSeqi | NP_001126361.1, NM_001132889.1 |
Genome annotation databases
GeneIDi | 100173342 |
KEGGi | pon:100173342 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR860178 mRNA Translation: CAH92320.1 |
RefSeqi | NP_001126361.1, NM_001132889.1 |
3D structure databases
BMRBi | Q5R7E0 |
SMRi | Q5R7E0 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9601.ENSPPYP00000000577 |
Protein family/group databases
PeroxiBasei | 4422, Ppy1CysPrx |
Genome annotation databases
GeneIDi | 100173342 |
KEGGi | pon:100173342 |
Organism-specific databases
CTDi | 9588 |
Phylogenomic databases
eggNOGi | KOG0854, Eukaryota |
InParanoidi | Q5R7E0 |
OrthoDBi | 1129256at2759 |
Family and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PRDX6_PONAB | |
Accessioni | Q5R7E0Primary (citable) accession number: Q5R7E0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 31, 2006 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 94 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families