ID A0A235B2Z4_9BACL Unreviewed; 218 AA.
AC A0A235B2Z4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
GN ORFNames=CHM34_15225 {ECO:0000313|EMBL:OYD06654.1};
OS Paludifilum halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Paludifilum.
OX NCBI_TaxID=1642702 {ECO:0000313|EMBL:OYD06654.1, ECO:0000313|Proteomes:UP000215459};
RN [1] {ECO:0000313|EMBL:OYD06654.1, ECO:0000313|Proteomes:UP000215459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102817 {ECO:0000313|EMBL:OYD06654.1,
RC ECO:0000313|Proteomes:UP000215459};
RA Belbahri L.;
RT "The genome sequence of Paludifilum halophilum highlights mechanisms for
RT microbial adaptation to high salt environemnts.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00401};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00401}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719, ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYD06654.1}.
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DR EMBL; NOWF01000010; OYD06654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235B2Z4; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000215459; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_00401};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00401};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00401};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_00401}; Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401};
KW Reference proteome {ECO:0000313|Proteomes:UP000215459}.
FT DOMAIN 14..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT ACT_SITE 55
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ SEQUENCE 218 AA; 24219 MW; DF43F21EEF1AC09E CRC64;
MSTEIETQAT PTLPKIGDPA PQFTAKTTQG EVSLSDYKGK WVLLFSHPAD FTPVCTTEFI
AFAKQNDEFA KRDVQLLGLS IDSLPAHLAW VNNIREKMGV EVPFPVIADL STAVAQKYGM
IHPEASETTT VRCVFVIDDK QVIRAIIYYP LNVGRNIDEV LRLVDALQTA DKHAVAAPAN
WRPGEEVVEP APQNDAGVKE RLKENTEGTD WYLKKKKL
//
