ID A0A061P030_9BACL Unreviewed; 167 AA.
AC A0A061P030;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Thiol peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
DE Short=Tpx {ECO:0000256|HAMAP-Rule:MF_00269};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Peroxiredoxin tpx {ECO:0000256|HAMAP-Rule:MF_00269};
DE Short=Prx {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00269};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00269};
GN Name=tpx {ECO:0000256|HAMAP-Rule:MF_00269};
GN ORFNames=JCM19038_3520 {ECO:0000313|EMBL:GAK09669.1};
OS Geomicrobium sp. JCM 19038.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK09669.1, ECO:0000313|Proteomes:UP000027014};
RN [1] {ECO:0000313|EMBL:GAK09669.1, ECO:0000313|Proteomes:UP000027014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK09669.1,
RC ECO:0000313|Proteomes:UP000027014};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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_00269}.
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_00269};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00269}.
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 atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000256|HAMAP-Rule:MF_00269}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00269}.
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:GAK09669.1}.
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DR EMBL; BAXA01000015; GAK09669.1; -; Genomic_DNA.
DR RefSeq; WP_042420177.1; NZ_BAXA01000015.1.
DR AlphaFoldDB; A0A061P030; -.
DR eggNOG; COG2077; Bacteria.
DR Proteomes; UP000027014; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR HAMAP; MF_00269; Tpx; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR InterPro; IPR018219; Tpx_CS.
DR PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS01265; TPX; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|HAMAP-
KW Rule:MF_00269}; Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00269};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_00269};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00269}; Reference proteome {ECO:0000313|Proteomes:UP000027014}.
FT DOMAIN 18..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 60
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
FT DISULFID 60..94
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00269"
SQ SEQUENCE 167 AA; 18465 MW; 8AA2F1F21A77EFCE CRC64;
MAKVTFKGNP MTLVGNEVKV GEQAPNFTVL DSSLQEKTLA DYEGKTIVIS VIPSIDTGVC
EQQTKRFNEE AAKLDNVQVL TISADLPFAQ KRWCAAEGVD NLEMLSDHRD FSFAQSFGLG
MKELRLLARA VFVIDDKGTI QHAEYVEEAT NHPDYDNALA QVNSLIK
//
