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1-Cys peroxiredoxin (EC 1.11.1.15) (Thiol-specific antioxidant) (Thioredoxin peroxidase)

 1CPX_ONCVO              Reviewed;         232 AA.
P52570;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
08-MAY-2019, entry version 69.
RecName: Full=1-Cys peroxiredoxin;
EC=1.11.1.15;
AltName: Full=Thiol-specific antioxidant;
AltName: Full=Thioredoxin peroxidase;
Name=TSA;
Onchocerca volvulus.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
NCBI_TaxID=6282;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Chandrashekar R., Curits K.C., Weil G.J.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 62-222.
Chandrashekar R., Curtis K., Weil G.J.;
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides.
{ECO:0000250|UniProtKB:O17433}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
+ an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
EC=1.11.1.15; Evidence={ECO:0000250|UniProtKB:O17433};
-!- 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. {ECO:0000250|UniProtKB:P34227}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000305}.
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EMBL; U31052; AAC27392.1; -; mRNA.
EMBL; U09385; AAA50214.2; -; mRNA.
SMR; P52570; -.
PeroxiBase; 4943; Ovo1CysPrx.
PRIDE; P52570; -.
Proteomes; UP000024404; Unassembled WGS sequence.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
2: Evidence at transcript level;
Antioxidant; Complete proteome; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome.
CHAIN 1 232 1-Cys peroxiredoxin.
/FTId=PRO_0000135105.
DOMAIN 5 176 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 49 49 {ECO:0000250}.
ACT_SITE 49 49 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P30041}.
SEQUENCE 232 AA; 25926 MW; 029E93F276232B37 CRC64;
MCAPSGPGNK FPDFQAETNE GFISSFYDWI GKDSWAILFS HPRDFTPVCT TELARLVQLA
PEFKKRNVKL IGLSCDSADS HSKWADDILA LYKMKCVGCD SEKKLPYPII ADEDRSLATE
LGMMDPDERD EKGNTLTARC VFIIGSDKTL KLSILYPATT GRNFDEILRV VDSLQLTAVK
LVATPVDWKD GDDCVVLPTI DDNEAKKLFG EKIHTIDLPS GKHYLRMVPH PK


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Related Genes :
[Prdx6 Aipla2 Aop2 Tsa] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein)
[PRDX6 AOP2 GPX PHGPX] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Ciliary body glutathione peroxidase) (Non-selenium glutathione peroxidase) (NSGPx) (PHGPx)
[Prdx6 Aop2 Ltw4 Prdx5] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx)
[PRDX6 AOP2 KIAA0106] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Liver 2D page spot 40) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)
[PRX1 YBL064C YBL0503 YBL0524] Peroxiredoxin PRX1, mitochondrial (Prx) (EC 1.11.1.15) (1-Cys PRX) (Mitochondrial thiol peroxidase) (mTPx) (Thioredoxin peroxidase)
[tpx Rv1932 MTCY09F9.32c] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (HBC189) (Peroxiredoxin III) (Prx-III) (Peroxiredoxin-3) (Protein MER5 homolog)
[PRXIIB TPX1 At1g65980 F12P19.14] Peroxiredoxin-2B (EC 1.11.1.15) (Peroxiredoxin IIB) (Peroxiredoxin TPx1) (Thioredoxin peroxidase 2B) (Thioredoxin-dependent peroxidase 1)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PRXIIF At3g06050 F24F17.3] Peroxiredoxin-2F, mitochondrial (EC 1.11.1.15) (Peroxiredoxin IIF) (Thioredoxin peroxidase 2F)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22)
[ahpC b0605 JW0598] Alkyl hydroperoxide reductase C (EC 1.11.1.15) (Alkyl hydroperoxide reductase protein C22) (Peroxiredoxin) (SCRP-23) (Sulfate starvation-induced protein 8) (SSI8) (Thioredoxin peroxidase)
[PRXIIE At3g52960 F8J2_130] Peroxiredoxin-2E, chloroplastic (EC 1.11.1.15) (Peroxiredoxin IIE) (Thioredoxin peroxidase 2E)
[ahpC Rv2428] Alkyl hydroperoxide reductase C (MtAhpC) (EC 1.11.1.15) (Peroxiredoxin) (Thioredoxin peroxidase)
[PRDX6 RCJMB04_18k11] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[HYR1 GPX3 ORP1 YIR037W] Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3)
[PER1 At1g48130 F21D18.15] 1-Cys peroxiredoxin PER1 (EC 1.11.1.15) (Rehydrin homolog) (Thioredoxin peroxidase)
[] Peroxiredoxin-2 (Prx) (EC 1.11.1.15) (1-Cys D-peroxiredoxin) (Peroxiredoxin II) (Thioredoxin peroxidase)
[ahpE Rv2238c MTCY427.19c] Alkyl hydroperoxide reductase E (EC 1.11.1.15) (Peroxiredoxin AhpE) (Prx) (Thioredoxin peroxidase) (TPx)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Fragments)
[GPX1 YKL026C] Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.15) (Glutathione peroxidase homolog 1) (GPx 1)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[GPX2 YBR244W YBR1632] Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.15) (Glutathione peroxidase homolog 2) (GPx 2)
[PRDX6 QtsA-11939] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[] Thioredoxin peroxidase (EC 1.11.1.15) (Peroxiredoxin) (Thiol-specific antioxidant protein) (Thioredoxin-dependent peroxide reductase)
[Os07g0638300 LOC_Os07g44430 OJ1340_C08.107 OsJ_024297] 1-Cys peroxiredoxin A (1-Cys Prx A) (EC 1.11.1.15) (Protein RAB24) (Rice 1Cys-peroxiredoxin) (R1C-Prx) (Thioredoxin peroxidase A)
[PRXIIC TPX2 At1g65970 F12P19.13] Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Peroxiredoxin TPx2) (Thioredoxin peroxidase 2C) (Thioredoxin-dependent peroxidase 2)
[GPX3 CAALFM_C107350CA orf19.4436] Glutathione peroxidase-like peroxiredoxin GPX3 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1); Non-structural protein 2 (nsp2); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10); Non-structural protein 11 (nsp11); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[DDB_G0282517] 1-Cys peroxiredoxin (EC 1.11.1.15) (Thiol-specific antioxidant) (Thioredoxin peroxidase)

Bibliography :
[25720803] Overexpression and activities of 1-Cys peroxiredoxin from Pseudomonas fluorescens GcM5-1A carried by pine wood nematode.
[22102027] Expression, purification, crystallization and preliminary X-ray crystallographic studies of alkyl hydroperoxide reductase (AhpC) from the cyanobacterium Anabaena sp. PCC 7120.
[17360337] Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C.
[12244436] A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker.
[10767529] FePer 1, a gene encoding an evolutionarily conserved 1-Cys peroxiredoxin in buckwheat (Fagopyrum esculentum Moench), is expressed in a seed-specific manner and induced during seed germination.
[10079938] [Study of structure of secretory 28 kDa protein from the rat olfactory epithelium].
[9783067] [Properties of the catalytic center of a secretory 28kDa protein (1-cys peroxiredoxin) from rat olfactory epithelium].