ID   A0A1C6VW03_9ACTN        Unreviewed;       155 AA.
AC   A0A1C6VW03;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Peroxiredoxin (Alkyl hydroperoxide reductase subunit C) {ECO:0000313|EMBL:SCL70473.1};
GN   ORFNames=GA0070603_5542 {ECO:0000313|EMBL:SCL70473.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL70473.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL70473.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL70473.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMIB01000002; SCL70473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6VW03; -.
DR   STRING; 47854.GA0070603_5542; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000198605; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd03018; PRX_AhpE_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR   PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..154
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        46
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   155 AA;  17252 MW;  8D1700041E386DBF CRC64;
     MPIEVGAEAP DFVLKDQNNQ EVRLADFRGR RTVLLVFYPL AFTGICQGEL CEVRDNLNEY
     VNEDVQVLTV SVDSVYAHKI WADREGYQFP LLADFWPHGA VAQAYGVFND VAGIANRGTF
     VIDKAGVVRF AEMNMPGEAR DQQGWRKALA EAVAA
//