ID A0A379MS07_9BACT Unreviewed; 197 AA.
AC A0A379MS07;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Probable peroxiredoxin {ECO:0000313|EMBL:SUE34303.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:SUE34303.1};
GN Name=tsaA {ECO:0000313|EMBL:SUE34303.1};
GN ORFNames=NCTC11190_01526 {ECO:0000313|EMBL:SUE34303.1};
OS Rikenella microfusus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Rikenella.
OX NCBI_TaxID=28139 {ECO:0000313|EMBL:SUE34303.1, ECO:0000313|Proteomes:UP000255233};
RN [1] {ECO:0000313|EMBL:SUE34303.1, ECO:0000313|Proteomes:UP000255233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11190 {ECO:0000313|EMBL:SUE34303.1,
RC ECO:0000313|Proteomes:UP000255233};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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. {ECO:0000256|ARBA:ARBA00037420}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR EMBL; UGVL01000001; SUE34303.1; -; Genomic_DNA.
DR RefSeq; WP_037291178.1; NZ_UGVL01000001.1.
DR AlphaFoldDB; A0A379MS07; -.
DR STRING; 880526.GCA_000427365_00035; -.
DR GeneID; 78539939; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000255233; Unassembled WGS sequence.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:RHEA.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF10417; 1-cysPrx_C; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SUE34303.1}; Peroxidase {ECO:0000313|EMBL:SUE34303.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255233}.
FT DOMAIN 3..177
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 197 AA; 21953 MW; 153972C44481B38A CRC64;
MSVLVGQKAP VFKAAAVING GEIVPEFSLE QYLGKKYVLF FFYPADFSAV CPTELLAFQR
LSEEFEKRNV AVVGCSGDSQ FVHQKWLSTP VKEGGIEGVQ YPLVADPSKT IMQNYDVLAG
DYLYSDNGEV AFRGPAMAYR GSFLIDKEGT VRHQVVNDLP LSRSTEETLR MIDALQHFEE
YGEACPIDWH QGDKGIK
//
