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Database: UniProt
Entry: Q6L1X5_PICTO
LinkDB: Q6L1X5_PICTO
Original site: Q6L1X5_PICTO 
ID   Q6L1X5_PICTO            Unreviewed;       150 AA.
AC   Q6L1X5; A0A8G2FWC8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000256|ARBA:ARBA00042163};
GN   OrderedLocusNames=PTO0442 {ECO:0000313|EMBL:AAT43027.1};
GN   ORFNames=SAMN02745355_0565 {ECO:0000313|EMBL:SMD30671.1};
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828 / KAW 2/3).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT43027.1, ECO:0000313|Proteomes:UP000000438};
RN   [1] {ECO:0000313|EMBL:AAT43027.1, ECO:0000313|Proteomes:UP000000438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC   {ECO:0000313|Proteomes:UP000000438}, and DSM 9790
RC   {ECO:0000313|EMBL:AAT43027.1};
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN   [2] {ECO:0000313|EMBL:AAT43027.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 9790 {ECO:0000313|EMBL:AAT43027.1};
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SMD30671.1, ECO:0000313|Proteomes:UP000192315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9789 {ECO:0000313|EMBL:SMD30671.1,
RC   ECO:0000313|Proteomes:UP000192315};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000280};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000256|ARBA:ARBA00004456}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00038489}.
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DR   EMBL; AE017261; AAT43027.1; -; Genomic_DNA.
DR   EMBL; FWYE01000001; SMD30671.1; -; Genomic_DNA.
DR   RefSeq; WP_011177243.1; NZ_FWYE01000001.1.
DR   AlphaFoldDB; Q6L1X5; -.
DR   STRING; 263820.PTO0442; -.
DR   PeroxiBase; 4370; PItoBCP02.
DR   PaxDb; 263820-PTO0442; -.
DR   GeneID; 2844919; -.
DR   KEGG; pto:PTO0442; -.
DR   PATRIC; fig|263820.9.peg.467; -.
DR   eggNOG; arCOG00310; Archaea.
DR   HOGENOM; CLU_042529_14_1_2; -.
DR   InParanoid; Q6L1X5; -.
DR   OrthoDB; 145578at2157; -.
DR   Proteomes; UP000000438; Chromosome.
DR   Proteomes; UP000192315; Unassembled WGS sequence.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03017; PRX_BCP; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192315};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT   DOMAIN          4..148
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   150 AA;  17055 MW;  240C904668B34A10 CRC64;
     MELLKVGDTA PDFETVDQNG KTVKLSDFRG MPVVLYFYPK DNTPGCTVEA KNFRDNMDIF
     DSRVKVIGVS VDSQESHMKF HEKLNLNFDL LSDKSKEIVK KYGVLGVSTA KRVTYIIDQN
     GKIAHVFEKV KPDGHAKEVY EKLKELKLIN
//
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