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Database: UniProt
Entry: A0A0A0D6J0_9PROT
LinkDB: A0A0A0D6J0_9PROT
Original site: A0A0A0D6J0_9PROT 
ID   A0A0A0D6J0_9PROT        Unreviewed;       179 AA.
AC   A0A0A0D6J0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462};
DE            EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021};
DE   AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077};
GN   ORFNames=P409_15695 {ECO:0000313|EMBL:KGM33458.1};
OS   Inquilinus limosus MP06.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Inquilinus.
OX   NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM33458.1, ECO:0000313|Proteomes:UP000029995};
RN   [1] {ECO:0000313|EMBL:KGM33458.1, ECO:0000313|Proteomes:UP000029995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP06 {ECO:0000313|EMBL:KGM33458.1,
RC   ECO:0000313|Proteomes:UP000029995};
RA   Pino M., Di Conza J., Gutkind G.;
RT   "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT   limosus.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00000318};
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:KGM33458.1}.
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DR   EMBL; JANX01000181; KGM33458.1; -; Genomic_DNA.
DR   RefSeq; WP_034838854.1; NZ_JANX01000181.1.
DR   AlphaFoldDB; A0A0A0D6J0; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000029995; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN 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          2..161
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   179 AA;  20051 MW;  1DCF9034977C6A1F CRC64;
     MLTIGDTFPD FSLQAVVSTN PKDAFTQIDR AASKGKWKVV FFWPKDFTFV CPTEIAAFGK
     LAGDFADRDA LVYGVSTDSE FVHLAWRQNH ADLKELPIPM LADIRKDLSR SLGILEPTEE
     VCLRATFIVD PDNIIRFVSV NDMSVGRNPQ EVLRVLDALQ TDELCPCNWQ KGEETLKAA
//
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