Alkyl hydroperoxide reductase subunit C - Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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P0A251 (AHPC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alkyl hydroperoxide reductase subunit C
EC=1.11.1.15

Alternative name(s):
Alkyl hydroperoxide reductase protein C22
Peroxiredoxin
Thioredoxin peroxidase

Gene names

Name:	ahpC
Ordered Locus Names:	STM0608

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation.
Post-translational modification	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.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to oxidative stress Inferred from electronic annotation. Source: InterPro
Molecular_function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 187

186

Alkyl hydroperoxide reductase subunit C

PRO_0000135120

Regions

Domain

2 – 157

156

Thioredoxin

Sites

Active site

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Disulfide bond

Interchain (with C-166); in linked form

Disulfide bond

166

Interchain (with C-47); in linked form

Experimental info

Sequence conflict

S → G AA sequence Ref.4

Sequence conflict

N → D AA sequence Ref.4

Sequence conflict

Q → N AA sequence Ref.4

Sequence conflict

K → H AA sequence Ref.4

Sequence conflict

E → H AA sequence Ref.4

Sequence conflict

E → S AA sequence Ref.4

Secondary structure

187

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A251 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 83B251C74DE9860D
Show »

FASTA

187

20,747

        10         20         30         40         50         60 
MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE 

        70         80         90        100        110        120 
LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR 

       130        140        150        160        170        180 
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAA HPGEVCPAKW KEGEATLAPS 


LDLVGKI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05478 Unassigned DNA. Translation: AAA16431.1.
AE006468 Genomic DNA. Translation: AAL19559.1.

PIR

A35441.

RefSeq

NP_459600.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A251.

SMR

P0A251. Positions 2-169.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM0608.

Protein family/group databases

PeroxiBase

4829. SetypAhpC.

Proteomic databases

PaxDb

P0A251.

PRIDE

P0A251.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL19559; AAL19559; STM0608.

GeneID

1252128.

KEGG

stm:STM0608.

PATRIC

32379561. VBISalEnt20916_0640.

Phylogenomic databases

eggNOG

COG0450.

HOGENOM

HOG000022343.

K03386.

OMA

FAHKAWH.

ProtClustDB

PRK10382.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR10681:SF7. PTHR10681:SF7. 1 hit.

Pfam

PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]

PIRSF

PIRSF000239. AHPC. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR03137. AhpC. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A251.

Entry information

Entry name

AHPC_SALTY

Accession

Primary (citable) accession number: P0A251
Secondary accession number(s): P19479

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents