UniProtKB - Q9MB35 (PERQ_SEDLI)
Protein
Peroxiredoxin Q, chloroplastic
Gene
PRXQ
Organism
Sedum lineare (Needle stonecrop)
Status
Functioni
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.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 atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.By similarity
Catalytic activityi
- EC:1.11.1.241 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 80 | Cysteine sulfenic acid (-SOH) intermediateBy similarity | 1 |
GO - Molecular functioni
- peroxidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-20842 |
Protein family/group databases
PeroxiBasei | 4304, SlinPrxQ |
Names & Taxonomyi
Protein namesi | Recommended name: Peroxiredoxin Q, chloroplastic (EC:1.11.1.241 Publication)Alternative name(s): Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin QCurated |
Gene namesi | Name:PRXQ |
Organismi | Sedum lineare (Needle stonecrop) |
Taxonomic identifieri | 114260 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › Saxifragales › Crassulaceae › Sedum |
Subcellular locationi
Chloroplast
- chloroplast thylakoid lumen By similarity
Chloroplast
- chloroplast thylakoid lumen Source: UniProtKB-SubCell
Keywords - Cellular componenti
Chloroplast, Plastid, ThylakoidPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | ‹1 – 36 | ChloroplastSequence analysisAdd BLAST | ›36 | |
ChainiPRO_5000049527 | 37 – 186 | Peroxiredoxin Q, chloroplasticAdd BLAST | 150 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 80 ↔ 85 | Redox-activeBy similarity |
Keywords - PTMi
Disulfide bondProteomic databases
PRIDEi | Q9MB35 |
Interactioni
Subunit structurei
Monomer.
1 PublicationFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 38 – 186 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 149 |
Sequence similaritiesi
Keywords - Domaini
Redox-active center, Transit peptideFamily and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00578, AhpC-TSA, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
i Sequence
Sequence statusi: Fragment.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9MB35-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
QTLQTSSQSQ FHGLKFSHAS SFKSPSAPLR KNSIFAKVTK GSTPPPFTLK
60 70 80 90 100
DQEGRPVSLS KFKGKPVVVY FYPADETPGC TKQACAFRDS YEKFKKAGAE
110 120 130 140 150
VVGISGDSSE SHKAFAKKYK LPFTLLSDEG NKVRKEWGVP SDLFGTLPGR
160 170 180
ETYVLDKNGV VQLVYNNQFQ PEKHIDETLK LLQSLK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB037598 mRNA Translation: BAA90524.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB037598 mRNA Translation: BAA90524.1 |
3D structure databases
SMRi | Q9MB35 |
ModBasei | Search... |
Protein family/group databases
PeroxiBasei | 4304, SlinPrxQ |
Proteomic databases
PRIDEi | Q9MB35 |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-20842 |
Family and domain databases
Gene3Di | 3.40.30.10, 1 hit |
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF00578, AhpC-TSA, 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 | PERQ_SEDLI | |
Accessioni | Q9MB35Primary (citable) accession number: Q9MB35 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 2007 |
Last sequence update: | October 1, 2000 | |
Last modified: | October 7, 2020 | |
This is version 76 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |