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Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)

 J0D7C9_HELPX            Unreviewed;       166 AA.
J0D7C9;
03-OCT-2012, integrated into UniProtKB/TrEMBL.
03-OCT-2012, sequence version 1.
25-OCT-2017, entry version 32.
RecName: Full=Thiol peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
Short=Tpx {ECO:0000256|HAMAP-Rule:MF_00269};
EC=1.11.1.15 {ECO:0000256|HAMAP-Rule:MF_00269};
AltName: Full=Peroxiredoxin tpx {ECO:0000256|HAMAP-Rule:MF_00269};
Short=Prx {ECO:0000256|HAMAP-Rule:MF_00269};
AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
Name=tpx {ECO:0000256|HAMAP-Rule:MF_00269};
ORFNames=HPHPH4_0641 {ECO:0000313|EMBL:EJB81768.1};
Helicobacter pylori Hp H-4.
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Helicobacteraceae; Helicobacter.
NCBI_TaxID=992060 {ECO:0000313|EMBL:EJB81768.1, ECO:0000313|Proteomes:UP000003170};
[1] {ECO:0000313|EMBL:EJB81768.1, ECO:0000313|Proteomes:UP000003170}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hp H-4 {ECO:0000313|EMBL:EJB81768.1,
ECO:0000313|Proteomes:UP000003170};
PubMed=23661595; DOI=10.1111/2049-632X.12045;
Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
"Genome sequences of 65 Helicobacter pylori strains isolated from
asymptomatic individuals and patients with gastric cancer, peptic
ulcer disease, or gastritis.";
Pathog. Dis. 68:39-43(2013).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides. {ECO:0000256|HAMAP-
Rule:MF_00269, ECO:0000256|SAAS:SAAS00860696}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000256|HAMAP-Rule:MF_00269, ECO:0000256|SAAS:SAAS00860695}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00860701}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in
the same subunit to form an intramolecular disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000256|HAMAP-Rule:MF_00269}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
{ECO:0000256|HAMAP-Rule:MF_00269, ECO:0000256|SAAS:SAAS00860699}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJB81768.1}.
-----------------------------------------------------------------------
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EMBL; AKOY01000002; EJB81768.1; -; Genomic_DNA.
RefSeq; WP_001174645.1; NZ_AKOY01000002.1.
ProteinModelPortal; J0D7C9; -.
EnsemblBacteria; EJB81768; EJB81768; HPHPH4_0641.
PATRIC; fig|992060.3.peg.622; -.
OrthoDB; POG091H06SC; -.
Proteomes; UP000003170; Unassembled WGS sequence.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
CDD; cd03014; PRX_Atyp2cys; 1.
HAMAP; MF_00269; Tpx; 1.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
InterPro; IPR002065; TPX.
InterPro; IPR018219; Tpx_CS.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
PROSITE; PS01265; TPX; 1.
3: Inferred from homology;
Antioxidant {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00735699};
Complete proteome {ECO:0000313|Proteomes:UP000003170};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00860694};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00735734, ECO:0000313|EMBL:EJB81768.1};
Peroxidase {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00735734, ECO:0000313|EMBL:EJB81768.1};
Redox-active center {ECO:0000256|HAMAP-Rule:MF_00269,
ECO:0000256|SAAS:SAAS00860700}.
DOMAIN 18 166 Thioredoxin.
{ECO:0000259|PROSITE:PS51352}.
ACT_SITE 60 60 Cysteine sulfenic acid (-SOH)
intermediate. {ECO:0000256|HAMAP-
Rule:MF_00269}.
DISULFID 60 94 Redox-active. {ECO:0000256|HAMAP-
Rule:MF_00269}.
SEQUENCE 166 AA; 18292 MW; 2EA73092689282A1 CRC64;
MQKVTFKEET YQLEGKALKV GDKAPDVKLV NGDLQEVNLL KQGVRFQVVS ALPSLTGSVC
LLQAKHFNEQ AGKLPSVSFS VISMDLPFSQ GQICGTEGIK DLRILSDFRY KAFGENYGVL
LGKGSLQGLL ARSVFVLDDK GVVIYKEIVQ NILEEPNYEA LLKVLK


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