ID A0A1M7LGR4_9FLAO Unreviewed; 197 AA.
AC A0A1M7LGR4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=SAMN05444484_109111 {ECO:0000313|EMBL:SHM77355.1};
OS Flavobacterium chilense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946677 {ECO:0000313|EMBL:SHM77355.1, ECO:0000313|Proteomes:UP000184028};
RN [1] {ECO:0000313|EMBL:SHM77355.1, ECO:0000313|Proteomes:UP000184028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24724 {ECO:0000313|EMBL:SHM77355.1,
RC ECO:0000313|Proteomes:UP000184028};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000256|ARBA:ARBA00003330}.
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 -!- 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; FRBT01000009; SHM77355.1; -; Genomic_DNA.
DR RefSeq; WP_068840596.1; NZ_LSYT01000001.1.
DR AlphaFoldDB; A0A1M7LGR4; -.
DR STRING; 946677.SAMN05444484_109111; -.
DR OrthoDB; 9809746at2; -.
DR Proteomes; UP000184028; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02970; PRX_like2; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..197
FT /note="thioredoxin-dependent peroxiredoxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009927915"
FT DOMAIN 32..197
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 197 AA; 21712 MW; E010E9FAE345942E CRC64;
MKKVFLIFLV ALSTVANAQT AIPKSANDIA PLLIGEKVPG ITLKTAENTA VKISDLLQKK
KTVLVFYRGG WCPYCNLHLQ ALAEAEKQIL DLGYQIIAIS PDSPENLKIT EEKDKVKYTL
LSDSKGELIK AMGIAYEVPE NYKSVINVHS KGINTSLLPV PSVFILNTEA DILFEYIAPD
FKHRITTDLL VSVLKAL
//
