ID A0A0U3MHN9_9MOLU Unreviewed; 150 AA.
AC A0A0U3MHN9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN ORFNames=ASO20_02730 {ECO:0000313|EMBL:ALV23550.1};
OS Mycoplasma sp. (ex Biomphalaria glabrata).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1749074 {ECO:0000313|EMBL:ALV23550.1, ECO:0000313|Proteomes:UP000063836};
RN [1] {ECO:0000313|Proteomes:UP000063836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Swain M.T., Geyer K., Niazi U., Hoffmann K.F.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALV23550.1, ECO:0000313|Proteomes:UP000063836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barreiro1 {ECO:0000313|EMBL:ALV23550.1};
RA Adema C.M.;
RT "Whole genome analysis of Biomphalaria glabrata (Mollusca, Lophotrochozoa),
RT a snail intermediate host for transmission of schistosomiasis.";
RL Submitted (JAN-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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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DR EMBL; CP013128; ALV23550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3MHN9; -.
DR STRING; 1749074.ASO20_02730; -.
DR KEGG; myg:ASO20_02730; -.
DR PATRIC; fig|1749074.3.peg.527; -.
DR Proteomes; UP000063836; 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:SF24; PEROXIREDOXIN BCP; 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:UP000063836}.
FT DOMAIN 3..150
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 150 AA; 17071 MW; BFEDE932DDBC296F CRC64;
MENKISIEIL AHKLLGSDQK EHCLNDYKGK YIVLYFYPMD NTPGCTIQGH KYTELLSKFE
ELNAVVIGVS KGNAAKKEGF AQKECYKHLL LADHPELVLS KYFGVTGKVF GLISRSSFII
SPDQEIIFSN KKVDHNDDAQ INYDFLKNHK
//
