Reviewed, UniProtKB/Swiss-Prot P0A251 (AHPC_SALTY)

Names and origin

Protein names

Recommended name:
    Alkyl hydroperoxide reductase subunit C
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin
    Thioredoxin peroxidase
    Alkyl hydroperoxide reductase protein C22

Gene names

Name:	ahpC
Ordered Locus Names:	STM0608

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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

1

1

Removed Ref.4

Chain

2 – 187

186

Alkyl hydroperoxide reductase subunit C

PRO_0000135120

Regions

Domain

2 – 157

156

Thioredoxin

Sites

Active site

47

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Disulfide bond

47

Interchain (with C-166); in linked form

Disulfide bond

166

Interchain (with C-47); in linked form

Experimental info

Sequence conflict

2

1

S → G AA sequence Ref.4

Sequence conflict

5

1

N → D AA sequence Ref.4

Sequence conflict

14

1

Q → N AA sequence Ref.4

Sequence conflict

17

1

K → H AA sequence Ref.4

Sequence conflict

20

1

E → H AA sequence Ref.4

Sequence conflict

23

1

E → S AA sequence Ref.4

Secondary structure

1

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187

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Beta strand

20 – 25

6

Helix

26 – 29

4

Beta strand

32 – 38

7

Helix

46 – 63

18

Beta strand

66 – 74

9

Helix

76 – 85

10

Helix

89 – 91

3

Beta strand

94 – 98

5

Helix

103 – 107

5

Turn

113 – 115

3

Beta strand

120 – 125

6

Beta strand

129 – 137

9

Helix

145 – 160

16

Turn

182 – 186

5

Sequences

	Sequence		Length	Mass (Da)
	P0A251-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 83B251C74DE9860D	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

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: 2191951] [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: 8041738] [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. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [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: 2643600] [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: 2693740] [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: 11969410] [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: 12714747] [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: 16060667] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05478 Unassigned DNA. Translation: AAA16431.1.
AE008724 Genomic DNA. Translation: AAL19559.1.

PIR

A35441.

RefSeq

NP_459600.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

4829. SetypAhpC.

Genome annotation databases

GeneID

1252128.

GenomeReviews

Gene locus STM0608 in contig AE006468_GR.

KEGG

stm:STM0608.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P0A251.

OMA

P0A251. GDLADHY.

Enzyme and pathway databases

BioCyc

STYP99287:STM0608-MON.

BRENDA

1.11.1.15. 2.

Family and domain databases

InterPro

IPR000866. Alkyl_hydroperoxide_Rdtase.
IPR017559. Peroxiredoxin.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

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

TIGRFAMs

TIGR03137. AhpC. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)