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Database: UniProt
Entry: I4BZY3_DESTA
LinkDB: I4BZY3_DESTA
Original site: I4BZY3_DESTA 
ID   I4BZY3_DESTA            Unreviewed;       236 AA.
AC   I4BZY3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:AFM22874.1};
GN   OrderedLocusNames=Desti_0126 {ECO:0000313|EMBL:AFM22874.1};
OS   Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC   Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC   Desulfomonilaceae; Desulfomonile.
OX   NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM22874.1, ECO:0000313|Proteomes:UP000006055};
RN   [1] {ECO:0000313|Proteomes:UP000006055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC   {ECO:0000313|Proteomes:UP000006055};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
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DR   EMBL; CP003360; AFM22874.1; -; Genomic_DNA.
DR   STRING; 706587.Desti_0126; -.
DR   KEGG; dti:Desti_0126; -.
DR   PATRIC; fig|706587.4.peg.144; -.
DR   eggNOG; COG0450; Bacteria.
DR   HOGENOM; CLU_042529_21_3_7; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000006055; Chromosome.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
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   NCBIfam; NF040737; peroxi_PrxU; 1.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW   Selenium {ECO:0000313|EMBL:AFM22874.1};
KW   Selenocysteine {ECO:0000313|EMBL:AFM22874.1}.
FT   DOMAIN          39..197
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   NON_STD         84
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000313|EMBL:AFM22874.1"
SQ   SEQUENCE   236 AA;  26027 MW;  A54D207F921A1F61 CRC64;
     MTQKVDGCVV PAKGPIRSKE ITEATGHAER KEEPIMTIAR VGRPAPDFEA SAYIENGFRN
     IKLSEFMGKW VVICFYPGDF TFVUPTELAT VAAKHDELVK MDVQVLSIST DSRFVHKIWD
     EEELSKMVPS GIPFAMLSDP GGEIGKVYGV YDEAAGVDIR GRFLIDPDGI IQAMEVMTPP
     VGRNFSELVR QVKAFQHVRQ SGGSEATPAG WKPGDPTLKP SPALVGKVWK EWKVSE
//
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