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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.
25-OCT-2017, entry version 26.
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: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{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_KK339370.1.
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; KFNAQAN; -.
PhylomeDB; P9WG35; -.
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; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA: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:InterPro.
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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