TDXH_NANEQ
ID TDXH_NANEQ Reviewed; 222 AA.
AC Q74NC6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 peroxidase {ECO:0000255|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401};
GN OrderedLocusNames=NEQ191;
OS Nanoarchaeum equitans (strain Kin4-M).
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanoarchaeaceae; Nanoarchaeum.
OX NCBI_TaxID=228908;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kin4-M;
RX PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA Stetter K.O., Short J.M., Noorderwier M.;
RT "The genome of Nanoarchaeum equitans: insights into early archaeal
RT evolution and derived parasitism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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. 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}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00401}.
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DR EMBL; AE017199; AAR39045.1; -; Genomic_DNA.
DR AlphaFoldDB; Q74NC6; -.
DR SMR; Q74NC6; -.
DR STRING; 228908.NEQ191; -.
DR EnsemblBacteria; AAR39045; AAR39045; NEQ191.
DR KEGG; neq:NEQ191; -.
DR PATRIC; fig|228908.8.peg.195; -.
DR HOGENOM; CLU_042529_4_4_2; -.
DR OMA; FWYPKDF; -.
DR BioCyc; NEQU228908:GJB6-206-MON; -.
DR Proteomes; UP000000578; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
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; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..222
FT /note="Peroxiredoxin"
FT /id="PRO_0000135160"
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 44
FT /note="Interchain (with C-217); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 211..217
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
FT DISULFID 217
FT /note="Interchain (with C-44); in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00401"
SQ SEQUENCE 222 AA; 25849 MW; 8C28CEE99B6313ED CRC64;
MVVLGQKFPE VEVQTTHGRM RLPDHYRGKW FVLFSHPADF TPVCTTEFVE FARNYDKFKA
MNTELIGLSI DQVFSHIKWI EWIKEKFNVE IPFPVIADDQ GELARMLGMI SPYKGTNTVR
AVFIVDPEGY IRAMLYYPQE TGRNIPEILR LVEALQTADK YGVATPANWH VDRYEFKPSS
IVGNDVIIPP ASSLEEKKDR EERAKKGEIE CFDWWFCHKK LE
