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

 TPX_MYCTU               Reviewed;         165 AA.
P9WG35; L0TB06; P66952; P95282;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
13-FEB-2019, entry version 31.
RecName: Full=Thiol peroxidase {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000303|PubMed:14871480};
Short=Tpx {ECO:0000255|HAMAP-Rule:MF_00269};
EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000269|PubMed:14871480};
AltName: Full=Peroxiredoxin tpx {ECO:0000255|HAMAP-Rule:MF_00269};
Short=Prx {ECO:0000255|HAMAP-Rule:MF_00269};
AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00269};
Name=tpx {ECO:0000255|HAMAP-Rule:MF_00269}; OrderedLocusNames=Rv1932;
ORFNames=MTCY09F9.32c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=14871480; DOI=10.1016/j.abb.2003.11.021;
Jaeger T., Budde H., Flohe L., Menge U., Singh M., Trujillo M.,
Radi R.;
"Multiple thioredoxin-mediated routes to detoxify hydroperoxides in
Mycobacterium tuberculosis.";
Arch. Biochem. Biophys. 423:182-191(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[4]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 3-165.
PubMed=16627951; DOI=10.1107/S0907444906008249;
Stehr M., Hecht H.J., Jaeger T., Flohe L., Singh M.;
"Structure of the inactive variant C60S of Mycobacterium tuberculosis
thiol peroxidase.";
Acta Crystallogr. D 62:563-567(2006).
[5]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
CYS-60; CYS-80 AND CYS-93.
PubMed=16884737; DOI=10.1016/j.jmb.2006.05.076;
Rho B.S., Hung L.W., Holton J.M., Vigil D., Kim S.I., Park M.S.,
Terwilliger T.C., Pedelacq J.D.;
"Functional and structural characterization of a thiol peroxidase from
Mycobacterium tuberculosis.";
J. Mol. Biol. 361:850-863(2006).
-!- 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:0000255|HAMAP-
Rule:MF_00269, ECO:0000269|PubMed:14871480}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-dithiol + an hydroperoxide = [protein]-
disulfide + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-
COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377,
ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
ChEBI:CHEBI:50058; EC=1.11.1.15; Evidence={ECO:0000255|HAMAP-
Rule:MF_00269, ECO:0000269|PubMed:14871480};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14.5 uM for tert-butyl hydroperoxide (using thioredoxin TrxB
as electron donor) {ECO:0000269|PubMed:14871480};
KM=184.5 uM for tert-butyl hydroperoxide (using thioredoxin TrxC
as electron donor) {ECO:0000269|PubMed:14871480};
KM=2.0 uM for TrxB (using tert-butyl hydroperoxide as substrate)
{ECO:0000269|PubMed:14871480};
KM=120.7 uM for TrxC (using tert-butyl hydroperoxide as
substrate) {ECO:0000269|PubMed:14871480};
Note=kcat is 0.70 sec(-1) with tert-butyl hydroperoxide as
substrate and TrxB as reductant and 11.1 sec(-1) with tert-butyl
hydroperoxide as substrate and TrxC as reductant.
{ECO:0000269|PubMed:14871480};
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00269,
ECO:0000269|PubMed:16884737}.
-!- 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 (TrxB and TrxC).
{ECO:0000255|HAMAP-Rule:MF_00269, ECO:0000305|PubMed:14871480}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
{ECO:0000255|HAMAP-Rule:MF_00269}.
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EMBL; AL123456; CCP44699.1; -; Genomic_DNA.
PIR; H70635; H70635.
RefSeq; NP_216448.1; NC_000962.3.
RefSeq; WP_003409700.1; NZ_NVQJ01000034.1.
PDB; 1XVQ; X-ray; 1.75 A; A=1-165.
PDB; 1Y25; X-ray; 2.10 A; A/B=3-165.
PDBsum; 1XVQ; -.
PDBsum; 1Y25; -.
ProteinModelPortal; P9WG35; -.
SMR; P9WG35; -.
STRING; 83332.Rv1932; -.
PaxDb; P9WG35; -.
EnsemblBacteria; CCP44699; CCP44699; Rv1932.
GeneID; 885357; -.
KEGG; mtu:Rv1932; -.
TubercuList; Rv1932; -.
eggNOG; ENOG4108V1J; Bacteria.
eggNOG; COG2077; LUCA.
KO; K11065; -.
OMA; ITQEPNY; -.
PhylomeDB; P9WG35; -.
BioCyc; MTBH37RV:G185E-6129-MONOMER; -.
Reactome; R-HSA-1222538; Tolerance by Mtb to nitric oxide produced by macrophages.
Reactome; R-HSA-1222541; Cell redox homeostasis.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; HDA:MTBBASE.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:MTBBASE.
GO; GO:0004601; F:peroxidase activity; IDA:MTBBASE.
GO; GO:0051920; F:peroxiredoxin activity; IDA:MTBBASE.
GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
GO; GO:0045454; P:cell redox homeostasis; IDA:MTBBASE.
GO; GO:0052060; P:evasion or tolerance by symbiont of host-produced nitric oxide; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IDA:MTBBASE.
GO; GO:0051409; P:response to nitrosative stress; IDA:MTBBASE.
GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
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.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Disulfide bond;
Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
CHAIN 1 165 Thiol peroxidase.
/FTId=PRO_0000187888.
DOMAIN 18 165 Thioredoxin. {ECO:0000255|HAMAP-
Rule:MF_00269}.
ACT_SITE 60 60 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P0A862,
ECO:0000255|HAMAP-Rule:MF_00269,
ECO:0000305|PubMed:16884737}.
DISULFID 60 93 Redox-active.
{ECO:0000250|UniProtKB:P0A862,
ECO:0000255|HAMAP-Rule:MF_00269,
ECO:0000305|PubMed:16884737}.
MUTAGEN 60 60 C->S: Abolishes catalytic activity.
{ECO:0000269|PubMed:16884737}.
MUTAGEN 80 80 C->S: Increases catalytic activity.
{ECO:0000269|PubMed:16884737}.
MUTAGEN 93 93 C->S: Abolishes catalytic activity.
{ECO:0000269|PubMed:16884737}.
STRAND 3 6 {ECO:0000244|PDB:1Y25}.
STRAND 13 15 {ECO:0000244|PDB:1XVQ}.
STRAND 28 30 {ECO:0000244|PDB:1XVQ}.
STRAND 36 38 {ECO:0000244|PDB:1XVQ}.
HELIX 39 42 {ECO:0000244|PDB:1XVQ}.
STRAND 47 51 {ECO:0000244|PDB:1XVQ}.
HELIX 62 73 {ECO:0000244|PDB:1XVQ}.
STRAND 77 84 {ECO:0000244|PDB:1XVQ}.
HELIX 86 89 {ECO:0000244|PDB:1XVQ}.
STRAND 101 105 {ECO:0000244|PDB:1XVQ}.
HELIX 111 114 {ECO:0000244|PDB:1XVQ}.
TURN 123 126 {ECO:0000244|PDB:1XVQ}.
STRAND 130 135 {ECO:0000244|PDB:1XVQ}.
STRAND 139 146 {ECO:0000244|PDB:1XVQ}.
HELIX 156 165 {ECO:0000244|PDB:1XVQ}.
SEQUENCE 165 AA; 16896 MW; B251D5DADE2286FE CRC64;
MAQITLRGNA INTVGELPAV GSPAPAFTLT GGDLGVISSD QFRGKSVLLN IFPSVDTPVC
ATSVRTFDER AAASGATVLC VSKDLPFAQK RFCGAEGTEN VMPASAFRDS FGEDYGVTIA
DGPMAGLLAR AIVVIGADGN VAYTELVPEI AQEPNYEAAL AALGA


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Related Genes :
[tpx Rv1932 MTCY09F9.32c] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[PRXIIB TPX1 At1g65980 F12P19.14] Peroxiredoxin-2B (EC 1.11.1.15) (Peroxiredoxin IIB) (Peroxiredoxin TPx1) (Thioredoxin peroxidase 2B) (Thioredoxin-dependent peroxidase 1)
[PRX1 YBL064C YBL0503 YBL0524] Peroxiredoxin PRX1, mitochondrial (Prx) (EC 1.11.1.15) (1-Cys PRX) (Mitochondrial thiol peroxidase) (mTPx) (Thioredoxin peroxidase)
[Prdx6 Aipla2 Aop2 Tsa] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein)
[PRDX6 AOP2 GPX PHGPX] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Ciliary body glutathione peroxidase) (Non-selenium glutathione peroxidase) (NSGPx) (PHGPx)
[PRDX6 AOP2 KIAA0106] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Liver 2D page spot 40) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)
[Prdx6 Aop2 Ltw4 Prdx5] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx)
[ahpE Rv2238c MTCY427.19c] Alkyl hydroperoxide reductase E (EC 1.11.1.15) (Peroxiredoxin AhpE) (Prx) (Thioredoxin peroxidase) (TPx)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PRXIIF At3g06050 F24F17.3] Peroxiredoxin-2F, mitochondrial (EC 1.11.1.15) (Peroxiredoxin IIF) (Thioredoxin peroxidase 2F)
[PRXIIE At3g52960 F8J2_130] Peroxiredoxin-2E, chloroplastic (EC 1.11.1.15) (Peroxiredoxin IIE) (Thioredoxin peroxidase 2E)
[PRXIIC TPX2 At1g65970 F12P19.13] Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Peroxiredoxin TPx2) (Thioredoxin peroxidase 2C) (Thioredoxin-dependent peroxidase 2)
[HYR1 GPX3 ORP1 YIR037W] Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3)
[PRDX6 RCJMB04_18k11] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[ahpC b0605 JW0598] Alkyl hydroperoxide reductase C (EC 1.11.1.15) (Alkyl hydroperoxide reductase protein C22) (Peroxiredoxin) (SCRP-23) (Sulfate starvation-induced protein 8) (SSI8) (Thioredoxin peroxidase)
[ahpC Rv2428] Alkyl hydroperoxide reductase C (MtAhpC) (EC 1.11.1.15) (Peroxiredoxin) (Thioredoxin peroxidase)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (HBC189) (Peroxiredoxin III) (Prx-III) (Peroxiredoxin-3) (Protein MER5 homolog)
[GPX1 YKL026C] Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.15) (Glutathione peroxidase homolog 1) (GPx 1)
[] Peroxiredoxin-2 (Prx) (EC 1.11.1.15) (1-Cys D-peroxiredoxin) (Peroxiredoxin II) (Thioredoxin peroxidase)
[GPX2 YBR244W YBR1632] Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.15) (Glutathione peroxidase homolog 2) (GPx 2)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PER1 At1g48130 F21D18.15] 1-Cys peroxiredoxin PER1 (EC 1.11.1.15) (Rehydrin homolog) (Thioredoxin peroxidase)
[PRDX6 QtsA-11939] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22)
[tpx OR1_00751] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[Os07g0638300 LOC_Os07g44430 OJ1340_C08.107 OsJ_024297] 1-Cys peroxiredoxin A (1-Cys Prx A) (EC 1.11.1.15) (Protein RAB24) (Rice 1Cys-peroxiredoxin) (R1C-Prx) (Thioredoxin peroxidase A)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Fragments)
[tpx OR16_32831] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[tpx OR214_03609] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[dyp1] Dye-decolorizing peroxidase AauDyP1 (EC 1.11.1.19) (EC 1.11.1.7) (AjP I) (Manganese-independent peroxidase I) [Cleaved into: Dye-decolorizing peroxidase AauDyP2 (EC 1.11.1.19) (EC 1.11.1.7) (AjP II) (Manganese-independent peroxidase II)]

Bibliography :
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