ID A0A1Q4HJT7_9MYCO Unreviewed; 164 AA.
AC A0A1Q4HJT7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BRW64_06090 {ECO:0000313|EMBL:OJZ67808.1}, BV510_07120
GN {ECO:0000313|EMBL:OPE55058.1}, CRI78_24265
GN {ECO:0000313|EMBL:PEG51884.1};
OS Mycolicibacterium diernhoferi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1801 {ECO:0000313|EMBL:OJZ67808.1, ECO:0000313|Proteomes:UP000186837};
RN [1] {ECO:0000313|EMBL:OPE55058.1, ECO:0000313|Proteomes:UP000191039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM1 {ECO:0000313|EMBL:OPE55058.1,
RC ECO:0000313|Proteomes:UP000191039};
RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RT "genome sequences of unsequenced Mycobacteria.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OJZ67808.1, ECO:0000313|Proteomes:UP000186837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bard {ECO:0000313|EMBL:OJZ67808.1,
RC ECO:0000313|Proteomes:UP000186837};
RA Greninger A.L., Fang F., Jerome K.R.;
RT "Genome sequences of unsequenced Mycobacteria.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PEG51884.1, ECO:0000313|Proteomes:UP000220340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP141170001 {ECO:0000313|EMBL:PEG51884.1,
RC ECO:0000313|Proteomes:UP000220340};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (OCT-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_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 -!- SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00269}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OJZ67808.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MPNS01000002; OJZ67808.1; -; Genomic_DNA.
DR EMBL; MIJD01000050; OPE55058.1; -; Genomic_DNA.
DR EMBL; PDCR01000041; PEG51884.1; -; Genomic_DNA.
DR RefSeq; WP_073855261.1; NZ_PDCR01000041.1.
DR AlphaFoldDB; A0A1Q4HJT7; -.
DR STRING; 1801.BRW64_06090; -.
DR OrthoDB; 9781543at2; -.
DR Proteomes; UP000186837; Unassembled WGS sequence.
DR Proteomes; UP000191039; Unassembled WGS sequence.
DR Proteomes; UP000220340; 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}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00269};
KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_00269, ECO:0000313|EMBL:OJZ67808.1};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00269}.
FT DOMAIN 18..164
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"
SQ SEQUENCE 164 AA; 16690 MW; 50ACDF718048C0B8 CRC64;
MAQITLKGNP INTVGELPAV GSPAPAFSLV GSDLGAVTSE QYSGKPVLLN IFPSVDTGIC
AASVRTFNER AAATGATVLN VSKDLPFAQA RFCGAEGIEN VGSASAFRDS FGEDYGITLA
DGPMAGLLGR AVVVIGADGN VAYTELVPEI VQEPNYDAAL AALQ
//
