TDXH_PYRHO
ID TDXH_PYRHO Reviewed; 216 AA.
AC O58966;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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:12944367, ECO:0000269|PubMed:15625325};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000255|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
GN Name=ahpC; OrderedLocusNames=PH1217;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-26, CATALYTIC ACTIVITY, FUNCTION, INDUCTION BY
RP OXYGEN, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=15625325; DOI=10.1093/jb/mvh157;
RA Kawakami R., Sakuraba H., Kamohara S., Goda S., Kawarabayasi Y.,
RA Ohshima T.;
RT "Oxidative stress response in an anaerobic hyperthermophilic archaeon:
RT presence of a functional peroxiredoxin in Pyrococcus horikoshii.";
RL J. Biochem. 136:541-547(2004).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, AND INDUCTION.
RX PubMed=12944367; DOI=10.1093/jb/mvg109;
RA Kashima Y., Ishikawa K.;
RT "Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from
RT Pyrococcus horikoshii.";
RL J. Biochem. 134:25-29(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=23832195; DOI=10.1107/s1744309113014036;
RA Nakamura T., Mori A., Niiyama M., Matsumura H., Tokuyama C., Morita J.,
RA Uegaki K., Inoue T.;
RT "Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon
RT Pyrococcus horikoshii.";
RL Acta Crystallogr. F 69:719-722(2013).
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:12944367, ECO:0000269|PubMed:15625325}.
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:12944367,
CC ECO:0000269|PubMed:15625325};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.8. {ECO:0000269|PubMed:15625325};
CC Temperature dependence:
CC Thermostable. Retains full activity after 20 minutes at 90 degrees
CC Celsius and 75 % of its initial activity after 20 minutes at 100
CC degrees Celsius. {ECO:0000269|PubMed:15625325};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000255|HAMAP-Rule:MF_00401,
CC ECO:0000269|PubMed:23832195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}.
CC -!- INDUCTION: Up-regulated by exposure to oxygen (at protein level).
CC {ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}.
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:0000250|UniProtKB:Q9Y9L0, ECO:0000255|HAMAP-Rule:MF_00401}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00401}.
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DR EMBL; BA000001; BAA30317.1; -; Genomic_DNA.
DR PIR; C71065; C71065.
DR RefSeq; WP_010885304.1; NC_000961.1.
DR PDB; 3W6G; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-216.
DR PDB; 5XBQ; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J/K/L=1-216.
DR PDB; 5XBR; X-ray; 2.10 A; A/B=1-216.
DR PDB; 6IU1; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-216.
DR PDBsum; 3W6G; -.
DR PDBsum; 5XBQ; -.
DR PDBsum; 5XBR; -.
DR PDBsum; 6IU1; -.
DR AlphaFoldDB; O58966; -.
DR SMR; O58966; -.
DR STRING; 70601.3257634; -.
DR PRIDE; O58966; -.
DR EnsemblBacteria; BAA30317; BAA30317; BAA30317.
DR GeneID; 1443539; -.
DR KEGG; pho:PH1217; -.
DR eggNOG; arCOG00312; Archaea.
DR OMA; FWYPKDF; -.
DR OrthoDB; 98508at2157; -.
DR BRENDA; 1.11.1.24; 5244.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0071453; P:cellular response to oxygen levels; IDA:UniProtKB.
DR CDD; cd03016; PRX_1cys; 1.
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; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15625325"
FT CHAIN 2..216
FT /note="Peroxiredoxin"
FT /id="PRO_0000135165"
FT DOMAIN 2..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401,
FT ECO:0000269|PubMed:23832195"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 46
FT /note="Interchain (with C-211); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 205..211
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 211
FT /note="Interchain (with C-46); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:5XBR"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5XBQ"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:5XBR"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:5XBR"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:5XBR"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3W6G"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5XBR"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5XBR"
SQ SEQUENCE 216 AA; 24757 MW; A95DF14BF3874CA9 CRC64;
MVVIGEKFPE VEVKTTHGVI KLPDYFTKQG KWFILFSHPA DFTPVCTTEF YGMQKRVEEF
RKLGVEPIGL SVDQVFSHIK WIEWIKDNLS VEIDFPVIAD DRGELAEKLG MIPSGATITA
RAVFVVDDKG IIRAIVYYPA EVGRDWDEIL RLVKALKIST EKGVALPHKW PNNELIGDKV
IVPPASTIEE KKQREEAKAK GEIECYDWWF CYKKLE
