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P0A251

- AHPC_SALTY

UniProt

P0A251 - AHPC_SALTY

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Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediate

GO - Molecular functioni

  1. peroxidase activity Source: UniProtKB-KW
  2. peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

  1. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciSENT99287:GCTI-611-MONOMER.

Protein family/group databases

PeroxiBasei4829. SetypAhpC.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit C (EC:1.11.1.15)
Alternative name(s):
Alkyl hydroperoxide reductase protein C22
Peroxiredoxin
Thioredoxin peroxidase
Gene namesi
Name:ahpC
Ordered Locus Names:STM0608
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 187186Alkyl hydroperoxide reductase subunit CPRO_0000135120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 – 47Interchain (with C-166); in linked form
Disulfide bondi166 – 166Interchain (with C-47); in linked form

Post-translational modificationi

The Cys-47-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0A251.
PRIDEiP0A251.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.

Protein-protein interaction databases

STRINGi99287.STM0608.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176
Beta strandi20 – 256
Helixi26 – 294
Beta strandi32 – 387
Beta strandi42 – 454
Helixi46 – 5611
Helixi58 – 636
Beta strandi66 – 749
Helixi76 – 8510
Helixi89 – 913
Beta strandi94 – 985
Helixi103 – 1075
Turni113 – 1153
Beta strandi120 – 1256
Beta strandi129 – 1379
Helixi145 – 16016
Turni182 – 1865

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N8JX-ray2.17A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
1YEPX-ray2.50A/B/C/D/E2-187[»]
1YEXX-ray2.30A/B/C/D/E2-187[»]
1YF0X-ray2.50A/B/C/D/E2-187[»]
1YF1X-ray2.60A/B/C/D/E/F/G/H/I/J2-187[»]
3EMPX-ray4.00A/B/C/D/E2-187[»]
4MA9X-ray1.82A/B/C/D/E2-187[»]
4MABX-ray1.90A/B/C/D/E2-187[»]
ProteinModelPortaliP0A251.
SMRiP0A251. Positions 2-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A251.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
KOiK03386.
OMAiPDEACPA.
OrthoDBiEOG67X1XH.
PhylomeDBiP0A251.

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.
[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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A251-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE
60 70 80 90 100
LGDVADHYEE LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP
110 120 130 140 150
TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR
160 170 180
KIKAAQYVAA HPGEVCPAKW KEGEATLAPS LDLVGKI
Length:187
Mass (Da):20,747
Last modified:January 23, 2007 - v2
Checksum:i83B251C74DE9860D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → G AA sequence (PubMed:2643600)Curated
Sequence conflicti5 – 51N → D AA sequence (PubMed:2643600)Curated
Sequence conflicti14 – 141Q → N AA sequence (PubMed:2643600)Curated
Sequence conflicti17 – 171K → H AA sequence (PubMed:2643600)Curated
Sequence conflicti20 – 201E → H AA sequence (PubMed:2643600)Curated
Sequence conflicti23 – 231E → S AA sequence (PubMed:2643600)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05478 Unassigned DNA. Translation: AAA16431.1.
AE006468 Genomic DNA. Translation: AAL19559.1.
PIRiA35441.
RefSeqiNP_459600.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19559; AAL19559; STM0608.
GeneIDi1252128.
KEGGistm:STM0608.
PATRICi32379561. VBISalEnt20916_0640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05478 Unassigned DNA. Translation: AAA16431.1 .
AE006468 Genomic DNA. Translation: AAL19559.1 .
PIRi A35441.
RefSeqi NP_459600.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N8J X-ray 2.17 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 2-187 [» ]
1YEP X-ray 2.50 A/B/C/D/E 2-187 [» ]
1YEX X-ray 2.30 A/B/C/D/E 2-187 [» ]
1YF0 X-ray 2.50 A/B/C/D/E 2-187 [» ]
1YF1 X-ray 2.60 A/B/C/D/E/F/G/H/I/J 2-187 [» ]
3EMP X-ray 4.00 A/B/C/D/E 2-187 [» ]
4MA9 X-ray 1.82 A/B/C/D/E 2-187 [» ]
4MAB X-ray 1.90 A/B/C/D/E 2-187 [» ]
ProteinModelPortali P0A251.
SMRi P0A251. Positions 2-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM0608.

Protein family/group databases

PeroxiBasei 4829. SetypAhpC.

Proteomic databases

PaxDbi P0A251.
PRIDEi P0A251.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL19559 ; AAL19559 ; STM0608 .
GeneIDi 1252128.
KEGGi stm:STM0608.
PATRICi 32379561. VBISalEnt20916_0640.

Phylogenomic databases

eggNOGi COG0450.
HOGENOMi HOG000022343.
KOi K03386.
OMAi PDEACPA.
OrthoDBi EOG67X1XH.
PhylomeDBi P0A251.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-611-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A251.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000239. AHPC. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR03137. AhpC. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases."
    Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.
    J. Biol. Chem. 265:10535-10540(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TN1379.
  2. "Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes."
    Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.
    Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  4. "An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties."
    Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N.
    J. Biol. Chem. 264:1488-1496(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-25.
    Strain: oxyR1.
  5. "Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress."
    Tartaglia L.A., Storz G., Ames B.N.
    J. Mol. Biol. 210:709-719(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins."
    Wood Z.A., Poole L.B., Hantgan R.R., Karplus P.A.
    Biochemistry 41:5493-5504(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  7. "Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling."
    Wood Z.A., Poole L.B., Karplus P.A.
    Science 300:650-653(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF MUTANT SER-47.
  8. "Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin."
    Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., Poole L.B.
    Biochemistry 44:10583-10592(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiAHPC_SALTY
AccessioniPrimary (citable) accession number: P0A251
Secondary accession number(s): P19479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3