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Protein

Peroxiredoxin

Gene

APE_2278

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protects cells against oxidative stress. Can reduce hydrogen peroxide using dithiothreitol as an electron donor (in vitro).1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Cysteine sulfenic acid (-SOH) intermediateUniRule annotation1 Publication
Binding sitei126 – 1261Substrate

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • peroxiredoxin activity Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: UniProtKB-HAMAP
  • cellular response to hydrogen peroxide Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Enzyme and pathway databases

BioCyciAPER272557:GJD6-1534-MONOMER.
BRENDAi1.11.1.15. 171.

Names & Taxonomyi

Protein namesi
Recommended name:
PeroxiredoxinUniRule annotation (EC:1.11.1.15UniRule annotation)
Alternative name(s):
Thioredoxin peroxidase
Short name:
ApTPx
Gene namesi
Ordered Locus Names:APE_2278
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
Proteomesi
  • UP000002518 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501C → S: Abolishes enzyme activity. 1 Publication
Mutagenesisi207 – 2071C → S: Reduces enzyme activity. 1 Publication
Mutagenesisi213 – 2131C → S: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250PeroxiredoxinPRO_0000135153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi207 ↔ 213Sequence analysis

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Up-regulated by hydrogen peroxide (at protein level).1 Publication

Interactioni

Subunit structurei

Homodecamer. Pentamer of dimers that assemble into a ring structure.UniRule annotation3 Publications

Protein-protein interaction databases

DIPiDIP-29934N.
STRINGi272557.APE_2278.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi15 – 195Combined sources
Beta strandi22 – 265Combined sources
Helixi28 – 314Combined sources
Turni32 – 343Combined sources
Beta strandi36 – 405Combined sources
Helixi48 – 5912Combined sources
Helixi61 – 666Combined sources
Beta strandi69 – 779Combined sources
Helixi79 – 9214Combined sources
Beta strandi101 – 1033Combined sources
Helixi105 – 1073Combined sources
Helixi108 – 1136Combined sources
Turni118 – 1203Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi135 – 1439Combined sources
Helixi151 – 16717Combined sources
Turni173 – 1764Combined sources
Turni179 – 1813Combined sources
Beta strandi185 – 1873Combined sources
Helixi193 – 20210Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi212 – 2154Combined sources
Helixi220 – 23415Combined sources
Helixi241 – 2433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0RX-ray2.00A/B/C/D/E/F/G/H/I/J2-250[»]
2CV4X-ray2.30A/B/C/D/E/F/G/H/I/J1-250[»]
2E2GX-ray2.40A/B/C/D/E/F/G/H/I/J1-250[»]
2E2MX-ray2.60A/B/C/D/E/F/G/H/I/J1-250[»]
2NVLX-ray2.36A/B/C/D/E/F/G/H/I/J1-250[»]
2ZCTX-ray1.70A/B/C/D/E/F/G/H/I/J2-250[»]
3A2VX-ray1.65A/B/C/D/E/F/G/H/I/J2-250[»]
3A2WX-ray2.30A/B/C/D/E/F/G/H/I/J2-250[»]
3A2XX-ray1.90A/B/C/D/E/F/G/H/I/J2-250[»]
3A5WX-ray2.20A/B/C/D/E/F/G/H/I/J2-250[»]
DisProtiDP00037.
ProteinModelPortaliQ9Y9L0.
SMRiQ9Y9L0. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y9L0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 163158ThioredoxinUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family. TDXH subfamily.UniRule annotation
Contains 1 thioredoxin domain.UniRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiarCOG00312. Archaea.
COG0450. LUCA.
HOGENOMiHOG000022346.
KOiK03386.
OMAiGEKFPEV.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_00401. Peroxiredoxin. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR022915. Peroxiredoxin_TDXH.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y9L0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGSIPLIGE RFPEMEVTTD HGVIKLPDHY VSQGKWFVLF SHPADFTPVC
60 70 80 90 100
TTEFVSFARR YEDFQRLGVD LIGLSVDSVF SHIKWKEWIE RHIGVRIPFP
110 120 130 140 150
IIADPQGTVA RRLGLLHAES ATHTVRGVFI VDARGVIRTM LYYPMELGRL
160 170 180 190 200
VDEILRIVKA LKLGDSLKRA VPADWPNNEI IGEGLIVPPP TTEDQARARM
210 220 230 240 250
ESGQYRCLDW WFCWDTPASR DDVEEARRYL RRAAEKPAKL LYEEARTHLH
Length:250
Mass (Da):28,703
Last modified:November 1, 1999 - v1
Checksum:i0457F2852D051E7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA81290.1.
PIRiB72454.

Genome annotation databases

EnsemblBacteriaiBAA81290; BAA81290; APE_2278.
KEGGiape:APE_2278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA81290.1.
PIRiB72454.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0RX-ray2.00A/B/C/D/E/F/G/H/I/J2-250[»]
2CV4X-ray2.30A/B/C/D/E/F/G/H/I/J1-250[»]
2E2GX-ray2.40A/B/C/D/E/F/G/H/I/J1-250[»]
2E2MX-ray2.60A/B/C/D/E/F/G/H/I/J1-250[»]
2NVLX-ray2.36A/B/C/D/E/F/G/H/I/J1-250[»]
2ZCTX-ray1.70A/B/C/D/E/F/G/H/I/J2-250[»]
3A2VX-ray1.65A/B/C/D/E/F/G/H/I/J2-250[»]
3A2WX-ray2.30A/B/C/D/E/F/G/H/I/J2-250[»]
3A2XX-ray1.90A/B/C/D/E/F/G/H/I/J2-250[»]
3A5WX-ray2.20A/B/C/D/E/F/G/H/I/J2-250[»]
DisProtiDP00037.
ProteinModelPortaliQ9Y9L0.
SMRiQ9Y9L0. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29934N.
STRINGi272557.APE_2278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA81290; BAA81290; APE_2278.
KEGGiape:APE_2278.

Phylogenomic databases

eggNOGiarCOG00312. Archaea.
COG0450. LUCA.
HOGENOMiHOG000022346.
KOiK03386.
OMAiGEKFPEV.

Enzyme and pathway databases

BioCyciAPER272557:GJD6-1534-MONOMER.
BRENDAi1.11.1.15. 171.

Miscellaneous databases

EvolutionaryTraceiQ9Y9L0.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_00401. Peroxiredoxin. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR022915. Peroxiredoxin_TDXH.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTDXH_AERPE
AccessioniPrimary (citable) accession number: Q9Y9L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.