ID W6ABV4_9MOLU Unreviewed; 141 AA.
AC W6ABV4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SSABA_v1c09210 {ECO:0000313|EMBL:AHI54320.1};
OS Spiroplasma sabaudiense Ar-1343.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276257 {ECO:0000313|EMBL:AHI54320.1, ECO:0000313|Proteomes:UP000019265};
RN [1] {ECO:0000313|EMBL:AHI54320.1, ECO:0000313|Proteomes:UP000019265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar-1343 {ECO:0000313|EMBL:AHI54320.1};
RX PubMed=24534435;
RA Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT "Molecular evolution of the substrate utilization strategies and putative
RT virulence factors in mosquito-associated Spiroplasma species.";
RL Genome Biol. Evol. 6:500-509(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 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; CP006934; AHI54320.1; -; Genomic_DNA.
DR RefSeq; WP_025251456.1; NZ_CP006934.1.
DR AlphaFoldDB; W6ABV4; -.
DR STRING; 1276257.SSABA_v1c09210; -.
DR KEGG; ssab:SSABA_v1c09210; -.
DR PATRIC; fig|1276257.3.peg.937; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_1_14; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000019265; Chromosome.
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:UP000019265};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 1..141
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 141 AA; 16042 MW; 2AD32320F72CA246 CRC64;
MNWKTKKYML ENSESKMLSE LTGQKGLVLF FYPVANADHC AMELKAYEKK AMAINDKGYN
VVGVSRDSVP EQEKFAKSCM INFSLISDSD LTLHNEFKVI TSTEPAEEDR STFILDNNLN
VLHELRSVDT SSHIDEVIMK L
//
