ID A0A0N1AI33_9SPHN Unreviewed; 185 AA.
AC A0A0N1AI33;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=IP65_15075 {ECO:0000313|EMBL:KPF52901.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF52901.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF52901.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF52901.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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}.
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:KPF52901.1}.
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DR EMBL; LJHO01000008; KPF52901.1; -; Genomic_DNA.
DR RefSeq; WP_022676314.1; NZ_LJHO01000008.1.
DR AlphaFoldDB; A0A0N1AI33; -.
DR STRING; 1523413.IP65_15075; -.
DR PATRIC; fig|1523413.3.peg.4118; -.
DR OrthoDB; 5572803at2; -.
DR Proteomes; UP000037880; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd03017; PRX_BCP; 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 Reference proteome {ECO:0000313|Proteomes:UP000037880};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..185
FT /note="thioredoxin-dependent peroxiredoxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005865760"
FT DOMAIN 27..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 185 AA; 19660 MW; 26C0AF39E69F6230 CRC64;
MNTRSPLAAL AAFALSLTPM AAAHAALPQG ARAPDFSAQG ALGGKPFSFN LKKALKRGPV
VLYFYPKAFT QGCTMEAHAF ADATADFARA GATVIGMSND DIATLTRFST EECRDKFAVA
AASPAVVRAY DVDLQQGGKS TGLTTRTSYV IAPDGRITLV HSDMDYRDHV RLTLAAVQAM
HRRHG
//
