PRX2_POPTR
ID PRX2_POPTR Reviewed; 162 AA.
AC A9PCL4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Peroxiredoxin-2 {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.25 {ECO:0000269|PubMed:11706208, ECO:0000269|PubMed:15032877};
DE AltName: Full=1-Cys D-peroxiredoxin {ECO:0000303|PubMed:16916801};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin II {ECO:0000303|PubMed:15032877};
DE AltName: Full=Thioredoxin peroxidase;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT clones and their utility for the discovery of genes responding to insect
RT feeding.";
RL BMC Genomics 9:57-57(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=11706208; DOI=10.1104/pp.010586;
RA Rouhier N., Gelhaye E., Sautiere P.E., Brun A., Laurent P., Tagu D.,
RA Gerard J., de Fay E., Meyer Y., Jacquot J.P.;
RT "Isolation and characterization of a new peroxiredoxin from poplar sieve
RT tubes that uses either glutaredoxin or thioredoxin as a proton donor.";
RL Plant Physiol. 127:1299-1309(2001).
RN [3]
RP ACTIVE SITE, AND MUTAGENESIS OF CYS-51 AND CYS-76.
RX PubMed=11832487; DOI=10.1074/jbc.m111489200;
RA Rouhier N., Gelhaye E., Jacquot J.P.;
RT "Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein
RT interaction and catalytic mechanism.";
RL J. Biol. Chem. 277:13609-13614(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF THR-48 AND ARG-129.
RX PubMed=15032877; DOI=10.1111/j.0031-9317.2004.0203.x;
RA Rouhier N., Gelhaye E., Corbier C., Jacquot J.P.;
RT "Active site mutagenesis and phospholipid hydroperoxide reductase activity
RT of poplar type II peroxiredoxin.";
RL Physiol. Plantarum 120:57-62(2004).
RN [5]
RP SUBUNIT.
RX PubMed=16916801; DOI=10.1074/jbc.m602188200;
RA Noguera-Mazon V., Lemoine J., Walker O., Rouhier N., Salvador A.,
RA Jacquot J.P., Lancelin J.M., Krimm I.;
RT "Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-
RT covalent homodimer.";
RL J. Biol. Chem. 281:31736-31742(2006).
RN [6] {ECO:0007744|PDB:1TP9}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS), AND SUBUNIT.
RX PubMed=15697201; DOI=10.1021/bi048226s;
RA Echalier A., Trivelli X., Corbier C., Rouhier N., Walker O., Tsan P.,
RA Jacquot J.P., Aubry A., Krimm I., Lancelin J.M.;
RT "Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin
RT glutaredoxin and thioredoxin dependent: a new insight into the
RT peroxiredoxin oligomerism.";
RL Biochemistry 44:1755-1767(2005).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Can reduce H(2)O(2) and short chain organic, fatty acid,
CC and phospholipid hydroperoxides. Plays a role in cell protection
CC against oxidative stress by detoxifying peroxides.
CC {ECO:0000269|PubMed:15032877, ECO:0000269|PubMed:18230180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-
CC COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.25;
CC Evidence={ECO:0000269|PubMed:11706208, ECO:0000269|PubMed:15032877};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for phosphatidylcholine hydroperoxide
CC {ECO:0000269|PubMed:15032877};
CC -!- SUBUNIT: Monomer (PubMed:11706208, PubMed:15697201). Homodimer
CC (PubMed:16916801, PubMed:15697201). Glutathionylation of C(P) causes
CC the dimer to dissociate. Subsequent reduction of the mixed disulfide
CC bond leads again to dimerization (PubMed:16916801).
CC {ECO:0000269|PubMed:11706208, ECO:0000269|PubMed:15697201,
CC ECO:0000269|PubMed:16916801}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC C(P) is reactivated by glutathionylation and subsequent reduction by
CC glutaredoxin (Grx), or by thioredoxin (Trx). Preferentially uses
CC glutaredoxin. {ECO:0000305|PubMed:11832487,
CC ECO:0000305|PubMed:18230180}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; EF146010; ABK94117.1; -; mRNA.
DR PDB; 1TP9; X-ray; 1.62 A; A/B/C/D=1-162.
DR PDBsum; 1TP9; -.
DR AlphaFoldDB; A9PCL4; -.
DR SMR; A9PCL4; -.
DR STRING; 3694.POPTR_0018s09030.1; -.
DR eggNOG; KOG0541; Eukaryota.
DR BRENDA; 1.11.1.24; 4982.
DR BRENDA; 1.11.1.25; 4982.
DR ExpressionAtlas; A9PCL4; differential.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Oxidoreductase; Peroxidase; Redox-active center.
FT CHAIN 1..162
FT /note="Peroxiredoxin-2"
FT /id="PRO_0000441073"
FT DOMAIN 4..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000269|PubMed:11832487,
FT ECO:0000305|PubMed:15697201"
FT MUTAGEN 48
FT /note="T->V: Reduces catalytic activity to less than 4%."
FT /evidence="ECO:0000269|PubMed:11832487"
FT MUTAGEN 51
FT /note="C->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:11832487"
FT MUTAGEN 76
FT /note="C->A: Reduces catalytic activity by 75%."
FT /evidence="ECO:0000269|PubMed:11832487"
FT MUTAGEN 129
FT /note="R->Q: Reduces catalytic activity to less than 4%."
FT /evidence="ECO:0000269|PubMed:11832487"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1TP9"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1TP9"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1TP9"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1TP9"
SQ SEQUENCE 162 AA; 17415 MW; D6F6F3DA98F89559 CRC64;
MAPIAVGDVL PDGKLAYFDE QDQLQEVSVH SLVAGKKVIL FGVPGAFTPT CSLKHVPGFI
EKAGELKSKG VTEILCISVN DPFVMKAWAK SYPENKHVKF LADGSATYTH ALGLELNLQE
KGLGTRSRRF ALLVDDLKVK AANIEGGGEF TVSSADDILK DL
