TDXH_AERPE
ID TDXH_AERPE Reviewed; 250 AA.
AC Q9Y9L0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12707274};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00401};
DE Short=ApTPx;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
GN OrderedLocusNames=APE_2278;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HYDROGEN
RP PEROXIDE, DISULFIDE BOND, AND MUTAGENESIS OF CYS-50; CYS-207 AND CYS-213.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=12707274; DOI=10.1074/jbc.m300618200;
RA Jeon S.J., Ishikawa K.;
RT "Characterization of novel hexadecameric thioredoxin peroxidase from
RT Aeropyrum pernix K1.";
RL J. Biol. Chem. 278:24174-24180(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), ACTIVE SITE, DISULFIDE BOND, AND
RP SUBUNIT.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=16214169; DOI=10.1016/j.jmb.2005.09.006;
RA Mizohata E., Sakai H., Fusatomi E., Terada T., Murayama K., Shirouzu M.,
RA Yokoyama S.;
RT "Crystal structure of an archaeal peroxiredoxin from the aerobic
RT hyperthermophilic crenarchaeon Aeropyrum pernix K1.";
RL J. Mol. Biol. 354:317-329(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT SER-207, AND SUBUNIT.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=16342268; DOI=10.1002/prot.20796;
RA Nakamura T., Yamamoto T., Inoue T., Matsumura H., Kobayashi A.,
RA Hagihara Y., Uegaki K., Ataka M., Kai Y., Ishikawa K.;
RT "Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic
RT archaeon Aeropyrum pernix K1.";
RL Proteins 62:822-826(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=18436649; DOI=10.1073/pnas.0709822105;
RA Nakamura T., Yamamoto T., Abe M., Matsumura H., Hagihara Y., Goto T.,
RA Yamaguchi T., Inoue T.;
RT "Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur
RT intermediate.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6238-6242(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF WILD-TYPE AND MUTANTS SER-50 AND
RP SER-207 IN COMPLEX WITH HYDROGEN PEROXIDE, AND DISULFIDE BOND.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=19819903; DOI=10.1093/jb/mvp154;
RA Nakamura T., Kado Y., Yamaguchi T., Matsumura H., Ishikawa K., Inoue T.;
RT "Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with
RT its substrate, hydrogen peroxide.";
RL J. Biochem. 147:109-115(2010).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000255|HAMAP-Rule:MF_00401,
CC ECO:0000269|PubMed:12707274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00401, ECO:0000269|PubMed:12707274};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000255|HAMAP-Rule:MF_00401,
CC ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:16342268,
CC ECO:0000269|PubMed:19819903}.
CC -!- INTERACTION:
CC Q9Y9L0; Q9Y9L0: APE_2278; NbExp=2; IntAct=EBI-15699349, EBI-15699349;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401,
CC ECO:0000269|PubMed:12707274}.
CC -!- INDUCTION: Up-regulated by hydrogen peroxide (at protein level).
CC {ECO:0000269|PubMed:12707274}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. Although the primary
CC sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC its catalytic properties resemble those of the typical 2-Cys Prxs and
CC C(R) is provided by the other dimeric subunit to form an intersubunit
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000305|PubMed:12707274,
CC ECO:0000305|PubMed:16214169}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000305}.
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DR EMBL; BA000002; BAA81290.1; -; Genomic_DNA.
DR PIR; B72454; B72454.
DR PDB; 1X0R; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 2CV4; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 2E2G; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 2E2M; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 2NVL; X-ray; 2.36 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 2ZCT; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 3A2V; X-ray; 1.65 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 3A2W; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 3A2X; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 3A5W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=2-250.
DR PDB; 5XBS; X-ray; 2.51 A; A/B/C/D=1-250.
DR PDB; 6KRK; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 6KRM; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 6KRP; X-ray; 1.89 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 6KRQ; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=2-245.
DR PDB; 6KRR; X-ray; 2.15 A; A/B/C/D=2-245.
DR PDB; 6KRS; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=4-245.
DR PDB; 7C87; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 7C89; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 7C8A; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=1-250.
DR PDB; 7CQJ; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-250.
DR PDBsum; 1X0R; -.
DR PDBsum; 2CV4; -.
DR PDBsum; 2E2G; -.
DR PDBsum; 2E2M; -.
DR PDBsum; 2NVL; -.
DR PDBsum; 2ZCT; -.
DR PDBsum; 3A2V; -.
DR PDBsum; 3A2W; -.
DR PDBsum; 3A2X; -.
DR PDBsum; 3A5W; -.
DR PDBsum; 5XBS; -.
DR PDBsum; 6KRK; -.
DR PDBsum; 6KRM; -.
DR PDBsum; 6KRP; -.
DR PDBsum; 6KRQ; -.
DR PDBsum; 6KRR; -.
DR PDBsum; 6KRS; -.
DR PDBsum; 7C87; -.
DR PDBsum; 7C89; -.
DR PDBsum; 7C8A; -.
DR PDBsum; 7CQJ; -.
DR AlphaFoldDB; Q9Y9L0; -.
DR SMR; Q9Y9L0; -.
DR DIP; DIP-29934N; -.
DR STRING; 272557.APE_2278; -.
DR EnsemblBacteria; BAA81290; BAA81290; APE_2278.
DR KEGG; ape:APE_2278; -.
DR PATRIC; fig|272557.25.peg.1519; -.
DR eggNOG; arCOG00312; Archaea.
DR OMA; FWYPKDF; -.
DR BRENDA; 1.11.1.24; 171.
DR EvolutionaryTrace; Q9Y9L0; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR CDD; cd03016; PRX_1cys; 1.
DR DisProt; DP00037; -.
DR HAMAP; MF_00401; Peroxiredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR022915; Peroxiredoxin_TDXH.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..250
FT /note="Peroxiredoxin"
FT /id="PRO_0000135153"
FT DOMAIN 6..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000269|PubMed:19819903"
FT DISULFID 50
FT /note="Interchain (with C-213); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000305|PubMed:12707274, ECO:0000305|PubMed:16214169"
FT DISULFID 207..213
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:19819903"
FT DISULFID 213
FT /note="Interchain (with C-50); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000305|PubMed:12707274, ECO:0000305|PubMed:16214169"
FT MUTAGEN 50
FT /note="C->S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12707274"
FT MUTAGEN 207
FT /note="C->S: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:12707274"
FT MUTAGEN 213
FT /note="C->S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12707274"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3A2V"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2ZCT"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:3A2V"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2NVL"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:3A2V"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:3A2V"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3A2V"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:3A2V"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3A2V"
SQ 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
