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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)DescriptionActionsGraphical viewLength
Active sitei50Cysteine sulfenic acid (-SOH) intermediateUniRule annotation1 Publication1
Binding sitei126Substrate1

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi50C → S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi207C → S: Reduces enzyme activity. 1 Publication1
Mutagenesisi213C → S: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001351531 – 250PeroxiredoxinAdd BLAST250

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi15 – 19Combined sources5
Beta strandi22 – 26Combined sources5
Helixi28 – 31Combined sources4
Turni32 – 34Combined sources3
Beta strandi36 – 40Combined sources5
Helixi48 – 59Combined sources12
Helixi61 – 66Combined sources6
Beta strandi69 – 77Combined sources9
Helixi79 – 92Combined sources14
Beta strandi101 – 103Combined sources3
Helixi105 – 107Combined sources3
Helixi108 – 113Combined sources6
Turni118 – 120Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi126 – 131Combined sources6
Beta strandi135 – 143Combined sources9
Helixi151 – 167Combined sources17
Turni173 – 176Combined sources4
Turni179 – 181Combined sources3
Beta strandi185 – 187Combined sources3
Helixi193 – 202Combined sources10
Beta strandi205 – 209Combined sources5
Beta strandi212 – 215Combined sources4
Helixi220 – 234Combined sources15
Helixi241 – 243Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y9L0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 163ThioredoxinUniRule annotationAdd BLAST158

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
PDB 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.
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

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: November 2, 2016
This is version 100 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.