TDXH_SACS2
ID TDXH_SACS2 Reviewed; 215 AA.
AC P95895;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
GN OrderedLocusNames=SSO2121; ORFNames=C02015, C02_016;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 -!- 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};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000255|HAMAP-Rule:MF_00401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}.
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. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {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; Y08256; CAA69447.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42300.1; -; Genomic_DNA.
DR PIR; S74033; S74033.
DR RefSeq; WP_009990153.1; NC_002754.1.
DR AlphaFoldDB; P95895; -.
DR SMR; P95895; -.
DR STRING; 273057.SSO2121; -.
DR EnsemblBacteria; AAK42300; AAK42300; SSO2121.
DR GeneID; 44130831; -.
DR KEGG; sso:SSO2121; -.
DR PATRIC; fig|273057.12.peg.2211; -.
DR eggNOG; arCOG00312; Archaea.
DR HOGENOM; CLU_042529_4_4_2; -.
DR InParanoid; P95895; -.
DR OMA; FWYPKDF; -.
DR PhylomeDB; P95895; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 3: Inferred from homology;
KW Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..215
FT /note="Peroxiredoxin"
FT /id="PRO_0000135169"
FT DOMAIN 7..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
SQ SEQUENCE 215 AA; 24745 MW; 5210477EF4C9607B CRC64;
MSEERIPLIG ERFPEMEVIT TQGRIKLPDD YKGRWFVLFS HPGDFTPVCT TEFYSFAKKY
EEFKKLNTEL IGLSVDSNIS HIEWIMWIEK NLKVEIPFPI IADPMGNVAK RLGMIHAQSS
TATVRAVFVV DDKGVVRLIL YYPMEIGRNI DEILRAIRAL QLVDKAGVVT PANWPNNELI
GDKVINPAPR TIKDAKMRLG QPFDWWFTYK EVKTT
