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Protein
Submitted name:

Alkyl hydroperoxide reductase C

Gene

ahpC

Organism
Amphibacillus xylanus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Protein family/group databases

PeroxiBasei4918. AxAhpC.

Names & Taxonomyi

Protein namesi
Submitted name:
Alkyl hydroperoxide reductase CImported
Gene namesi
Name:ahpCImported
OrganismiAmphibacillus xylanusImported
Taxonomic identifieri1449 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeAmphibacillus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 – 48Interchain (with C-167)Combined sources
Disulfide bondi167 – 167Interchain (with C-48)Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WE0X-ray2.90A/B/C/D/E/F/G/H/I/J2-188[»]
ProteinModelPortaliO87200.
SMRiO87200. Positions 2-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO87200.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 158157ThioredoxinInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
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.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O87200-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLIGTEVQP FRAQAFQSGK DFFEVTEADL KGKWSIVVFY PADFSFVCPT
60 70 80 90 100
ELEDVQKEYA ELKKLGVEVY SVSTDTHFVH KAWHENSPAV GSIEYIMIGD
110 120 130 140 150
PSQTISRQFD VLNEETGLAD RGTFIIDPDG VIQAIEINAD GIGRDASTLI
160 170 180
NKVKAAQYVR ENPGEVCPAK WEEGGETLKP SLDIVGKI
Length:188
Mass (Da):20,774
Last modified:November 1, 1998 - v1
Checksum:iE61BA53C0215BA84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018435 Genomic DNA. Translation: BAA33808.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018435 Genomic DNA. Translation: BAA33808.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WE0X-ray2.90A/B/C/D/E/F/G/H/I/J2-188[»]
ProteinModelPortaliO87200.
SMRiO87200. Positions 2-167.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei4918. AxAhpC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO87200.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
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.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus."
    Niimura Y., Nishiyama Y., Saito D., Tsuji H., Hidaka M., Miyaji T., Watanabe T., Massey V.
    J. Bacteriol. 182:5046-5051(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Ep01Imported.
  2. "Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus xylanus."
    Kitano K., Kita A., Hakoshima T., Niimura Y., Miki K.
    Proteins 59:644-647(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-188, DISULFIDE BONDS.

Entry informationi

Entry nameiO87200_9BACI
AccessioniPrimary (citable) accession number: O87200
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.