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Peroxiredoxin (EC 1.11.1.15) (Thioredoxin peroxidase) (ApTPx)

 TDXH_AERPE              Reviewed;         250 AA.
Q9Y9L0;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 109.
RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_00401};
AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00401};
Short=ApTPx;
OrderedLocusNames=APE_2278;
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC
100138 / K1).
Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
Desulfurococcaceae; Aeropyrum.
NCBI_TaxID=272557;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=10382966; DOI=10.1093/dnares/6.2.83;
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H.,
Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y.,
Nomura N., Sako Y., Kikuchi H.;
"Complete genome sequence of an aerobic hyper-thermophilic
crenarchaeon, Aeropyrum pernix K1.";
DNA Res. 6:83-101(1999).
[2]
CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY
HYDROGEN PEROXIDE, DISULFIDE BOND, AND MUTAGENESIS OF CYS-50; CYS-207
AND CYS-213.
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=12707274; DOI=10.1074/jbc.M300618200;
Jeon S.J., Ishikawa K.;
"Characterization of novel hexadecameric thioredoxin peroxidase from
Aeropyrum pernix K1.";
J. Biol. Chem. 278:24174-24180(2003).
[3]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), ACTIVE SITE, DISULFIDE BOND,
AND SUBUNIT.
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=16214169; DOI=10.1016/j.jmb.2005.09.006;
Mizohata E., Sakai H., Fusatomi E., Terada T., Murayama K.,
Shirouzu M., Yokoyama S.;
"Crystal structure of an archaeal peroxiredoxin from the aerobic
hyperthermophilic crenarchaeon Aeropyrum pernix K1.";
J. Mol. Biol. 354:317-329(2005).
[4]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT SER-207, AND SUBUNIT.
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=16342268; DOI=10.1002/prot.20796;
Nakamura T., Yamamoto T., Inoue T., Matsumura H., Kobayashi A.,
Hagihara Y., Uegaki K., Ataka M., Kai Y., Ishikawa K.;
"Crystal structure of thioredoxin peroxidase from aerobic
hyperthermophilic archaeon Aeropyrum pernix K1.";
Proteins 62:822-826(2006).
[5]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND ACTIVE SITE.
PubMed=18436649; DOI=10.1073/pnas.0709822105;
Nakamura T., Yamamoto T., Abe M., Matsumura H., Hagihara Y., Goto T.,
Yamaguchi T., Inoue T.;
"Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur
intermediate.";
Proc. Natl. Acad. Sci. U.S.A. 105:6238-6242(2008).
[6]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF WILD-TYPE AND MUTANTS SER-50
AND SER-207 IN COMPLEX WITH HYDROGEN PEROXIDE, AND DISULFIDE BOND.
STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
PubMed=19819903; DOI=10.1093/jb/mvp154;
Nakamura T., Kado Y., Yamaguchi T., Matsumura H., Ishikawa K.,
Inoue T.;
"Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed
with its substrate, hydrogen peroxide.";
J. Biochem. 147:109-115(2010).
-!- 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_00401, ECO:0000269|PubMed:12707274}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274}.
-!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
structure. {ECO:0000255|HAMAP-Rule:MF_00401,
ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:16342268,
ECO:0000269|PubMed:19819903}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15699349, EBI-15699349;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401,
ECO:0000269|PubMed:12707274}.
-!- INDUCTION: Up-regulated by hydrogen peroxide (at protein level).
{ECO:0000269|PubMed:12707274}.
-!- 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. Although the primary sequence of this enzyme is similar to
those of the 1-Cys Prx6 enzymes, its catalytic properties resemble
those of the typical 2-Cys Prxs and C(R) is provided by the other
dimeric subunit to form an intersubunit disulfide. The disulfide
is subsequently reduced by thioredoxin. {ECO:0000255|HAMAP-
Rule:MF_00401, ECO:0000305|PubMed:12707274,
ECO:0000305|PubMed:16214169}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000305}.
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EMBL; BA000002; BAA81290.1; -; Genomic_DNA.
PIR; B72454; B72454.
PDB; 1X0R; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 2CV4; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=1-250.
PDB; 2E2G; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-250.
PDB; 2E2M; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-250.
PDB; 2NVL; X-ray; 2.36 A; A/B/C/D/E/F/G/H/I/J=1-250.
PDB; 2ZCT; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 3A2V; X-ray; 1.65 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 3A2W; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 3A2X; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 3A5W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=2-250.
PDB; 5XBS; X-ray; 2.51 A; A/B/C/D=1-250.
PDBsum; 1X0R; -.
PDBsum; 2CV4; -.
PDBsum; 2E2G; -.
PDBsum; 2E2M; -.
PDBsum; 2NVL; -.
PDBsum; 2ZCT; -.
PDBsum; 3A2V; -.
PDBsum; 3A2W; -.
PDBsum; 3A2X; -.
PDBsum; 3A5W; -.
PDBsum; 5XBS; -.
DisProt; DP00037; -.
ProteinModelPortal; Q9Y9L0; -.
SMR; Q9Y9L0; -.
DIP; DIP-29934N; -.
STRING; 272557.APE_2278; -.
PRIDE; Q9Y9L0; -.
EnsemblBacteria; BAA81290; BAA81290; APE_2278.
KEGG; ape:APE_2278; -.
PATRIC; fig|272557.25.peg.1519; -.
eggNOG; arCOG00312; Archaea.
eggNOG; COG0450; LUCA.
HOGENOM; HOG000022346; -.
KO; K03386; -.
OMA; CPANWEE; -.
OrthoDB; POG093Z0BGG; -.
BioCyc; APER272557:GJD6-1533-MONOMER; -.
BRENDA; 1.11.1.15; 171.
EvolutionaryTrace; Q9Y9L0; -.
Proteomes; UP000002518; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
HAMAP; MF_00401; Peroxiredoxin; 1.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR022915; Peroxiredoxin_TDXH.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
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;
Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center;
Reference proteome.
CHAIN 1 250 Peroxiredoxin.
/FTId=PRO_0000135153.
DOMAIN 6 163 Thioredoxin. {ECO:0000255|HAMAP-
Rule:MF_00401}.
ACT_SITE 50 50 Cysteine sulfenic acid (-SOH)
intermediate. {ECO:0000255|HAMAP-
Rule:MF_00401,
ECO:0000269|PubMed:16214169,
ECO:0000269|PubMed:18436649}.
BINDING 126 126 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00401,
ECO:0000269|PubMed:19819903}.
DISULFID 50 50 Interchain (with C-213); in linked form.
{ECO:0000255|HAMAP-Rule:MF_00401,
ECO:0000305|PubMed:12707274,
ECO:0000305|PubMed:16214169}.
DISULFID 207 213 Alternate. {ECO:0000255|HAMAP-
Rule:MF_00401,
ECO:0000269|PubMed:16214169,
ECO:0000269|PubMed:19819903}.
DISULFID 213 213 Interchain (with C-50); in linked form.
{ECO:0000255|HAMAP-Rule:MF_00401,
ECO:0000305|PubMed:12707274,
ECO:0000305|PubMed:16214169}.
MUTAGEN 50 50 C->S: Abolishes enzyme activity.
{ECO:0000269|PubMed:12707274}.
MUTAGEN 207 207 C->S: Reduces enzyme activity.
{ECO:0000269|PubMed:12707274}.
MUTAGEN 213 213 C->S: Abolishes enzyme activity.
{ECO:0000269|PubMed:12707274}.
STRAND 3 5 {ECO:0000244|PDB:3A2V}.
STRAND 15 19 {ECO:0000244|PDB:3A2V}.
STRAND 22 26 {ECO:0000244|PDB:3A2V}.
HELIX 28 31 {ECO:0000244|PDB:3A2V}.
TURN 32 34 {ECO:0000244|PDB:3A2V}.
STRAND 36 40 {ECO:0000244|PDB:3A2V}.
HELIX 48 59 {ECO:0000244|PDB:3A2V}.
HELIX 61 66 {ECO:0000244|PDB:3A2V}.
STRAND 69 77 {ECO:0000244|PDB:3A2V}.
HELIX 79 92 {ECO:0000244|PDB:3A2V}.
STRAND 101 103 {ECO:0000244|PDB:3A2V}.
HELIX 105 107 {ECO:0000244|PDB:2ZCT}.
HELIX 108 113 {ECO:0000244|PDB:3A2V}.
TURN 118 120 {ECO:0000244|PDB:2NVL}.
STRAND 121 123 {ECO:0000244|PDB:3A2V}.
STRAND 126 131 {ECO:0000244|PDB:3A2V}.
STRAND 135 143 {ECO:0000244|PDB:3A2V}.
HELIX 151 167 {ECO:0000244|PDB:3A2V}.
TURN 173 176 {ECO:0000244|PDB:3A2V}.
TURN 179 181 {ECO:0000244|PDB:3A2V}.
STRAND 185 187 {ECO:0000244|PDB:3A2V}.
HELIX 193 202 {ECO:0000244|PDB:3A2V}.
STRAND 205 209 {ECO:0000244|PDB:3A2V}.
STRAND 212 215 {ECO:0000244|PDB:3A2V}.
HELIX 220 234 {ECO:0000244|PDB:3A2V}.
HELIX 241 243 {ECO:0000244|PDB:3A2V}.
SEQUENCE 250 AA; 28703 MW; 0457F2852D051E7A CRC64;
MPGSIPLIGE RFPEMEVTTD HGVIKLPDHY VSQGKWFVLF SHPADFTPVC TTEFVSFARR
YEDFQRLGVD LIGLSVDSVF SHIKWKEWIE RHIGVRIPFP IIADPQGTVA RRLGLLHAES
ATHTVRGVFI VDARGVIRTM LYYPMELGRL VDEILRIVKA LKLGDSLKRA VPADWPNNEI
IGEGLIVPPP TTEDQARARM ESGQYRCLDW WFCWDTPASR DDVEEARRYL RRAAEKPAKL
LYEEARTHLH


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