PRXQ_WHEAT
ID PRXQ_WHEAT Reviewed; 217 AA.
AC Q5S1S6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Peroxiredoxin Q, chloroplastic;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q9LU86};
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000305};
DE Flags: Precursor;
GN Name=PRX1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li A.L., Meng C.S., Jia J.Z.;
RT "Isolation and identification of a gene in response to powdery mildew
RT disease in wheat.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000250|UniProtKB:Q9LU86}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q9LU86};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9LU86}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000250|UniProtKB:Q9LU86}.
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 atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P0AE52}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AY789643; AAV66923.1; -; mRNA.
DR AlphaFoldDB; Q5S1S6; -.
DR SMR; Q5S1S6; -.
DR STRING; 4565.Traes_7DS_A9BD8001C.1; -.
DR PeroxiBase; 4307; TaPrxQ.
DR PRIDE; Q5S1S6; -.
DR eggNOG; KOG0855; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q5S1S6; baseline and differential.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Chloroplast; Disulfide bond; Oxidoreductase; Peroxidase;
KW Plastid; Redox-active center; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..217
FT /note="Peroxiredoxin Q, chloroplastic"
FT /id="PRO_0000285114"
FT DOMAIN 70..217
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 112
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
FT DISULFID 112..117
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
SQ SEQUENCE 217 AA; 23364 MW; 9326DFED9E3DC18B CRC64;
MAFAASTACC KPSALLAPRA SSSSPPSQAR LCRPSTSAAF HGLRAPASAF ALAPAPRRRA
ASTGIVCGKV SKGSVPPNFT LKDQDGKTVS LSKFKGKPVV LYFYPADETP GCTKQACAFR
DSYEKYKKAG AEVIGISGDD AASHKAFAKK YRLPFTLLSD EGNKVRKEWG VPSDLFGTLP
GRQTYVLDKK GVVQYIYNNQ FQPEKHIGET LKIIQNL
