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Alkyl hydroperoxide reductase C (MtAhpC) (EC 1.11.1.15) (Peroxiredoxin) (Thioredoxin peroxidase)

 AHPC_MYCTU              Reviewed;         195 AA.
P9WQB7; L0T9L3; Q79FE2; Q7BHK8; Q7D758;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=Alkyl hydroperoxide reductase C;
Short=MtAhpC;
EC=1.11.1.15 {ECO:0000269|PubMed:12084012, ECO:0000269|PubMed:14871480};
AltName: Full=Peroxiredoxin;
AltName: Full=Thioredoxin peroxidase;
Name=ahpC; OrderedLocusNames=Rv2428;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7604044; DOI=10.1073/pnas.92.14.6625;
Sherman D.R., Sabo P.J., Hickey M.J., Arain T.M., Mahairas G.G.,
Yuan Y., Barry C.E. III, Stover C.K.;
"Disparate responses to oxidative stress in saprophytic and pathogenic
mycobacteria.";
Proc. Natl. Acad. Sci. U.S.A. 92:6625-6629(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=8596438; DOI=10.1111/j.1365-2958.1995.mmi_17050889.x;
Deretic V., Philipp W., Dhandayuthapani S., Mudd M.H., Curcic R.,
Garbe T., Heym B., Via L.E., Cole S.T.;
"Mycobacterium tuberculosis is a natural mutant with an inactivated
oxidative-stress regulatory gene: implications for sensitivity to
isoniazid.";
Mol. Microbiol. 17:889-900(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=An01, F07, Rm23, Rm24, and Rm30;
Orru G., Iona E., Memmi G., Oggioni M.R., Fattorini L., Orefici G.,
Pozzi G.;
"Mutation associated with isoniazid resistance in Italian isolates of
Mycobacterium tuberculosis.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
PROTEIN SEQUENCE OF 2-16, LACK OF ACTION ON ISONIAZID, AND INDUCTION
IN DRUG-RESISTANT BACTERIA.
STRAIN=ATCC 35822;
PubMed=8658136; DOI=10.1126/science.272.5268.1641;
Sherman D.R., Mdluli K., Hickey M.J., Arain T.M., Morris S.L.,
Barry C.E. III, Stover C.K.;
"Compensatory ahpC gene expression in isoniazid-resistant
Mycobacterium tuberculosis.";
Science 272:1641-1643(1996).
[6]
FUNCTION, MUTAGENESIS OF CYS-61; CYS-174 AND CYS-176, AND DISULFIDE
BOND.
PubMed=10766746; DOI=10.1074/jbc.M001001200;
Hillas P.J., del Alba F.S., Oyarzabal J., Wilks A.,
Ortiz De Montellano P.R.;
"The AhpC and AhpD antioxidant defense system of Mycobacterium
tuberculosis.";
J. Biol. Chem. 275:18801-18809(2000).
[7]
SUBUNIT.
PubMed=11171096;
Chauhan R., Mande S.C.;
"Characterization of the Mycobacterium tuberculosis H37Rv alkyl
hydroperoxidase AhpC points to the importance of ionic interactions in
oligomerization and activity.";
Biochem. J. 354:209-215(2001).
[8]
INDUCTION BY HYPOXIA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11416222; DOI=10.1073/pnas.121172498;
Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
Schoolnik G.K.;
"Regulation of the Mycobacterium tuberculosis hypoxic response gene
encoding alpha -crystallin.";
Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
[9]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FUNCTION AS ANTIOXIDANT,
MUTAGENESIS OF CYS-61; CYS-174; CYS-176 AND 174-CYS--CYS-176, AND
DISULFIDE BOND.
PubMed=12084012; DOI=10.1042/BJ20020545;
Chauhan R., Mande S.C.;
"Site-directed mutagenesis reveals a novel catalytic mechanism of
Mycobacterium tuberculosis alkylhydroperoxidase C.";
Biochem. J. 367:255-261(2002).
[10]
FUNCTION, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11799204; DOI=10.1126/science.1067798;
Bryk R., Lima C.D., Erdjument-Bromage H., Tempst P., Nathan C.;
"Metabolic enzymes of mycobacteria linked to antioxidant defense by a
thioredoxin-like protein.";
Science 295:1073-1077(2002).
[11]
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).
[12]
MUTAGENESIS OF CYS-61; CYS-174 AND CYS-176, AND DISULFIDE BOND.
PubMed=15178486; DOI=10.1016/j.abb.2004.04.017;
Koshkin A., Knudsen G.M., Ortiz De Montellano P.R.;
"Intermolecular interactions in the AhpC/AhpD antioxidant defense
system of Mycobacterium tuberculosis.";
Arch. Biochem. Biophys. 427:41-47(2004).
[13]
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT SER-176, DISULFIDE
BONDS, POSSIBLE CATALYTIC MECHANISM, AND SUBUNIT.
PubMed=15886207; DOI=10.1074/jbc.M503076200;
Guimaraes B.G., Souchon H., Honore N., Saint-Joanis B., Brosch R.,
Shepard W., Cole S.T., Alzari P.M.;
"Structure and mechanism of the alkyl hydroperoxidase AhpC, a key
element of the Mycobacterium tuberculosis defense system against
oxidative stress.";
J. Biol. Chem. 280:25735-25742(2005).
-!- 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. Together with AhpD,
DlaT and Lpd, constitutes an NADH-dependent peroxidase active
against hydrogen and alkyl peroxides as well as serving as a
peroxynitrite reductase, thus protecting the bacterium against
reactive nitrogen intermediates and oxidative stress generated by
the host immune system. Does not however seem to play a role in
detoxification of isoniazid. {ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:11799204, ECO:0000269|PubMed:12084012}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:12084012, ECO:0000269|PubMed:14871480}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.38 mM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:12084012};
KM=0.2 uM for tert-butyl hydroperoxide (using AhpD as electron
donor) {ECO:0000269|PubMed:14871480};
KM=5.1 uM for tert-butyl hydroperoxide (using thioredoxin TrxC
as electron donor) {ECO:0000269|PubMed:14871480};
KM=65.7 uM for AhpD (using tert-butyl hydroperoxide as
substrate) {ECO:0000269|PubMed:14871480};
KM=5.6 uM for TrxC (using tert-butyl hydroperoxide as substrate)
{ECO:0000269|PubMed:14871480};
Note=kcat is 0.6 sec(-1) with tert-butyl hydroperoxide as
substrate and AhpD as reductant and 0.1 sec(-1) with tert-butyl
hydroperoxide as substrate and TrxC as reductant.
{ECO:0000269|PubMed:14871480};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
assemble to form a ring-like dodecamer (PubMed:11171096,
PubMed:15886207). Identified in a complex with AhpD, DlaT and Lpd
(PubMed:11799204). {ECO:0000269|PubMed:11171096,
ECO:0000269|PubMed:11799204, ECO:0000269|PubMed:15886207}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
-!- INDUCTION: Induced in isoniazid (INH)-resistant, KatG-deficient
strains as well as in INH-sensitive strains when challenged with
the drug. Increased expression in these strains probably
compensates for loss of katG activity in detoxification of organic
peroxides. A possible member of the dormancy regulon. Induced in
response to reduced oxygen tension (hypoxia). It is hoped that
this regulon will give insight into the latent, or dormant phase
of infection. {ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:8658136}.
-!- 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 typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide
(PubMed:15178486, PubMed:15886207). The disulfide can subsequently
be reduced through a mixed disulfide with the C-terminal cysteine
of AhpD, resolved by its second cysteine (PubMed:15178486) or by
thioredoxin (TrxC) (PubMed:14871480).
{ECO:0000269|PubMed:14871480, ECO:0000269|PubMed:15178486,
ECO:0000305|PubMed:15886207}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U18264; AAA79919.1; -; Genomic_DNA.
EMBL; U16243; AAC43585.1; -; Genomic_DNA.
EMBL; AF313459; AAG34172.1; -; Genomic_DNA.
EMBL; AF313460; AAG34173.1; -; Genomic_DNA.
EMBL; AF313461; AAG34174.1; -; Genomic_DNA.
EMBL; AF313462; AAG34175.1; -; Genomic_DNA.
EMBL; AF313463; AAG34176.1; -; Genomic_DNA.
EMBL; AL123456; CCP45220.1; -; Genomic_DNA.
RefSeq; NP_216944.1; NC_000962.3.
RefSeq; WP_003412529.1; NZ_KK339370.1.
PDB; 2BMX; X-ray; 2.40 A; A/B/C=1-195.
PDBsum; 2BMX; -.
ProteinModelPortal; P9WQB7; -.
SMR; P9WQB7; -.
STRING; 83332.Rv2428; -.
PaxDb; P9WQB7; -.
EnsemblBacteria; CCP45220; CCP45220; Rv2428.
GeneID; 885717; -.
KEGG; mtu:Rv2428; -.
KEGG; mtv:RVBD_2428; -.
PATRIC; fig|83332.111.peg.2715; -.
TubercuList; Rv2428; -.
eggNOG; ENOG4105D3R; Bacteria.
eggNOG; COG0450; LUCA.
KO; K03386; -.
OMA; CPANWEE; -.
PhylomeDB; P9WQB7; -.
Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
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:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IDA:MTBBASE.
GO; GO:0032843; F:hydroperoxide reductase activity; IDA:MTBBASE.
GO; GO:0016491; F:oxidoreductase activity; IDA:MTBBASE.
GO; GO:0004601; F:peroxidase activity; IDA:MTBBASE.
GO; GO:0051920; F:peroxiredoxin activity; IDA:MTBBASE.
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:0052059; P:evasion or tolerance by symbiont of host-produced reactive oxygen species; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:MTBBASE.
GO; GO:0051409; P:response to nitrosative stress; IMP:MTBBASE.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome; Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8658136}.
CHAIN 2 195 Alkyl hydroperoxide reductase C.
/FTId=PRO_0000392913.
DOMAIN 4 170 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 61 61 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:10766746,
ECO:0000305|PubMed:12084012,
ECO:0000305|PubMed:15178486}.
DISULFID 61 61 Interchain (with C-133 in AhpD);
transient. {ECO:0000269|PubMed:15178486}.
DISULFID 61 61 Interchain (with C-174); in linked form.
{ECO:0000244|PDB:2BMX,
ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:15178486,
ECO:0000269|PubMed:15886207}.
DISULFID 174 174 Interchain (with C-61); in linked form.
{ECO:0000244|PDB:2BMX,
ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:15178486,
ECO:0000269|PubMed:15886207}.
MUTAGEN 61 61 C->A,S: No enzyme activity.
{ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:12084012,
ECO:0000269|PubMed:15178486}.
MUTAGEN 174 176 CAC->AAA: 50% reduction in oxidation
activity of dithiothreitol and 60%
reduction in oxidation of thiocyanate.
{ECO:0000269|PubMed:12084012}.
MUTAGEN 174 174 C->A: Very poor oxidation activity of
dithiothreitol and thiocyanate.
{ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:12084012,
ECO:0000269|PubMed:15178486}.
MUTAGEN 174 174 C->S: In reconstituted in vitro system
retains no enzyme activity.
{ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:12084012,
ECO:0000269|PubMed:15178486}.
MUTAGEN 176 176 C->A: 50% reduction in oxidation activity
of dithiothreitol and thiocyanate.
{ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:12084012,
ECO:0000269|PubMed:15178486}.
MUTAGEN 176 176 C->S: Retains about 10% activity with
tert-butylhydroperoxide. In reconstituted
in vitro system retains 30% enzyme
activity. {ECO:0000269|PubMed:10766746,
ECO:0000269|PubMed:12084012,
ECO:0000269|PubMed:15178486}.
STRAND 14 18 {ECO:0000244|PDB:2BMX}.
HELIX 23 25 {ECO:0000244|PDB:2BMX}.
HELIX 31 34 {ECO:0000244|PDB:2BMX}.
STRAND 35 39 {ECO:0000244|PDB:2BMX}.
STRAND 47 52 {ECO:0000244|PDB:2BMX}.
HELIX 62 70 {ECO:0000244|PDB:2BMX}.
HELIX 72 76 {ECO:0000244|PDB:2BMX}.
TURN 77 79 {ECO:0000244|PDB:2BMX}.
STRAND 80 88 {ECO:0000244|PDB:2BMX}.
HELIX 90 99 {ECO:0000244|PDB:2BMX}.
HELIX 103 105 {ECO:0000244|PDB:2BMX}.
STRAND 110 112 {ECO:0000244|PDB:2BMX}.
HELIX 117 121 {ECO:0000244|PDB:2BMX}.
STRAND 129 131 {ECO:0000244|PDB:2BMX}.
STRAND 133 138 {ECO:0000244|PDB:2BMX}.
STRAND 142 150 {ECO:0000244|PDB:2BMX}.
HELIX 158 169 {ECO:0000244|PDB:2BMX}.
HELIX 175 177 {ECO:0000244|PDB:2BMX}.
SEQUENCE 195 AA; 21566 MW; 011C1014F07C7095 CRC64;
MPLLTIGDQF PAYQLTALIG GDLSKVDAKQ PGDYFTTITS DEHPGKWRVV FFWPKDFTFV
CPTEIAAFSK LNDEFEDRDA QILGVSIDSE FAHFQWRAQH NDLKTLPFPM LSDIKRELSQ
AAGVLNADGV ADRVTFIVDP NNEIQFVSAT AGSVGRNVDE VLRVLDALQS DELCACNWRK
GDPTLDAGEL LKASA


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