TDXH1_CALS4
ID TDXH1_CALS4 Reviewed; 215 AA.
AC Q8RCY5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Peroxiredoxin 1 {ECO:0000255|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 1 {ECO:0000255|HAMAP-Rule:MF_00401};
GN OrderedLocusNames=TTE0270;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM23566.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008691; AAM23566.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8RCY5; -.
DR SMR; Q8RCY5; -.
DR STRING; 273068.TTE0270; -.
DR EnsemblBacteria; AAM23566; AAM23566; TTE0270.
DR KEGG; tte:TTE0270; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_4_4_9; -.
DR OMA; MIDYQDT; -.
DR Proteomes; UP000000555; 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; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..215
FT /note="Peroxiredoxin 1"
FT /id="PRO_0000135178"
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"
SQ SEQUENCE 215 AA; 24639 MW; 671C79BD53121E57 CRC64;
MKLLGEKFPS MEVMTTHGVK RLPEDYAGKW FVLFSHPADF TPVCTTEFVE FARKAEEFKQ
LNTELIGLSV DQVFSHIKWV EWIKDNTGVQ IPFPVIADEL GRVSNQLGMI HPGKGTNTVR
AVFIVDDKGV IRLIMYYPQE VGRNVDEILR ALKALQTADQ YGVALPEKWP NNYLIKDHVI
VPPSTDEASA NERKEKIKAK EIEAFDWWFV HKPLK
