UniProtKB - O24364 (BAS1_SPIOL)
Protein
2-Cys peroxiredoxin BAS1, chloroplastic
Gene
BAS1
Organism
Spinacia oleracea (Spinach)
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. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.By similarity
Catalytic activityi
- EC:1.11.1.15By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 119 | Cysteine sulfenic acid (-SOH) intermediateBy similarity | 1 |
GO - Molecular functioni
- peroxidase activity Source: UniProtKB-KW
- peroxiredoxin activity Source: UniProtKB-EC
GO - Biological processi
- cell redox homeostasis Source: InterPro
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Protein family/group databases
PeroxiBasei | 4408 So2CysPrx |
Names & Taxonomyi
Protein namesi | Recommended name: 2-Cys peroxiredoxin BAS1, chloroplastic (EC:1.11.1.15)Alternative name(s): Thiol-specific antioxidant protein |
Gene namesi | Name:BAS1 |
Organismi | Spinacia oleracea (Spinach) |
Taxonomic identifieri | 3562 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › Caryophyllales › Chenopodiaceae › Chenopodioideae › Anserineae › Spinacia |
Subcellular locationi
Chloroplast
- chloroplast By similarity
Chloroplast
- chloroplast Source: UniProtKB-SubCell
Other locations
- cell Source: GOC
Keywords - Cellular componenti
Chloroplast, PlastidPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 65 | ChloroplastBy similarityAdd BLAST | 65 | |
ChainiPRO_0000023786 | 66 – 265 | 2-Cys peroxiredoxin BAS1, chloroplasticAdd BLAST | 200 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 119 | Interchain (with C-240); in linked formBy similarity | ||
Disulfide bondi | 240 | Interchain (with C-119); in linked formBy similarity |
Keywords - PTMi
Disulfide bondInteractioni
Subunit structurei
Homodimer; disulfide-linked, upon oxidation.
By similarityProtein-protein interaction databases
IntActi | O24364, 1 interactor |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 73 – 232 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 160 |
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 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: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O24364-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MACVASSTTL ISSPSSRVFP AKSSLSSPSV SFLRTLSSPS ASASLRSGFA
60 70 80 90 100
RRSSLSSTSR RSFAVKAQAD DLPLVGNKAP DFEAEAVFDQ EFIKVKLSDY
110 120 130 140 150
IGKKYVILFF YPLDFTFVCP TEITAFSDRH SEFEKLNTEV LGVSVDSVFS
160 170 180 190 200
HLAWVQTDRK SGGLGDLNYP LISDVTKSIS KSFGVLIHDQ GIALRGLFII
210 220 230 240 250
DKEGVIQHST INNLGIGRSV DETMRTLQAL QYTGNPDEVC PAGWKPGEKS
260
MKPDPKLSKE YFSAI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X94219 mRNA Translation: CAA63910.1 |
PIRi | T09211 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X94219 mRNA Translation: CAA63910.1 |
PIRi | T09211 |
3D structure databases
SMRi | O24364 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | O24364, 1 interactor |
Protein family/group databases
PeroxiBasei | 4408 So2CysPrx |
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 | BAS1_SPIOL | |
Accessioni | O24364Primary (citable) accession number: O24364 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | January 1, 1998 | |
Last modified: | November 13, 2019 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |