UniProtKB - P52571 (REHY_BROSE)
Protein
Probable 1-Cys peroxiredoxin
Gene
N/A
Organism
Bromus secalinus (Rye brome)
Status
Functioni
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (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.By similarity
Catalytic activityi
- EC:1.11.1.24By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 30 | Cysteine sulfenic acid (-SOH) intermediateBy similarity | 1 |
GO - Molecular functioni
- peroxidase activity Source: UniProtKB-KW
- peroxiredoxin activity Source: InterPro
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Protein family/group databases
PeroxiBasei | 4976, Bse1CysPrx |
Names & Taxonomyi
Protein namesi | Recommended name: Probable 1-Cys peroxiredoxin (EC:1.11.1.24By similarity)Alternative name(s): Dormancy-associated protein PBS128 Rehydrin homolog Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxinCurated |
Organismi | Bromus secalinus (Rye brome) |
Taxonomic identifieri | 4502 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Poaceae › BOP clade › Pooideae › Bromeae › Bromus |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000135108 | ‹1 – 202 | Probable 1-Cys peroxiredoxinAdd BLAST | ›202 |
Expressioni
Tissue specificityi
Embryos.
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | ‹1 – 148 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | ›148 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 178 – 201 | Bipartite nuclear localization signalSequence analysisAdd BLAST | 24 |
Sequence similaritiesi
Keywords - Domaini
Redox-active centerFamily 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: Fragment.
P52571-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
STHGKIRIHD YVANGYVILF SHPGDFTPVC TTELAAMANY AKEFEKRGVK
60 70 80 90 100
LLGISCDDVQ SHKEWTKDIE AYKPGSKVTY PIMADPDRSA IKQLNMVDPD
110 120 130 140 150
EKDAEGQLPS RTLHIVGPDK KVKLSFLYPS CTGRNMDEVV RAVDSLLTAA
160 170 180 190 200
KHKVATPANW KPGECVVIAP GVSDEEAKKL FPQGFETKDL PSKKGYLRFT
KV
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 | X63202 mRNA Translation: CAA44884.1 |
PIRi | S22499 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X63202 mRNA Translation: CAA44884.1 |
PIRi | S22499 |
3D structure databases
SMRi | P52571 |
ModBasei | Search... |
Protein family/group databases
PeroxiBasei | 4976, Bse1CysPrx |
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 | REHY_BROSE | |
Accessioni | P52571Primary (citable) accession number: P52571 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | August 12, 2020 | |
This is version 82 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |