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Database: UniProt
Entry: K0NIA1_DESTT
LinkDB: K0NIA1_DESTT
Original site: K0NIA1_DESTT 
ID   K0NIA1_DESTT            Unreviewed;       199 AA.
AC   K0NIA1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Thioredoxin peroxidase {ECO:0000313|EMBL:CCK81091.1};
DE            EC=1.11.1.15 {ECO:0000313|EMBL:CCK81091.1};
GN   OrderedLocusNames=TOL2_C29320 {ECO:0000313|EMBL:CCK81091.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK81091.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK81091.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
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DR   EMBL; FO203503; CCK81091.1; -; Genomic_DNA.
DR   RefSeq; WP_014958300.1; NC_018645.1.
DR   AlphaFoldDB; K0NIA1; -.
DR   STRING; 651182.TOL2_C29320; -.
DR   KEGG; dto:TOL2_C29320; -.
DR   PATRIC; fig|651182.5.peg.3475; -.
DR   HOGENOM; CLU_042529_14_2_7; -.
DR   OrthoDB; 9809746at2; -.
DR   Proteomes; UP000007347; Chromosome.
DR   GO; GO:0004601; F:peroxidase 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; 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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CCK81091.1};
KW   Peroxidase {ECO:0000313|EMBL:CCK81091.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..199
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003835167"
FT   DOMAIN          48..199
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   199 AA;  22252 MW;  FFF5D74287049BD3 CRC64;
     MNSKKTFIVG ILILLIGYST SANTGSVAYG NKIYDPGKLK PVDSRLKVKI GDKAPDFVLP
     SIAGKPVRLS SFQGKKNLML TFIPAAWTPV CSDQWPGYNI AQDLFEQYDT HLLGISADNL
     PTLFAWTREM GGLWFEVLSD FWPHGDVSSA YGVLRTDGMS ERAIFLIDKK GIIRFIYVDD
     INRRPDLGMI VNQLKKLTF
//
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