ID   B2U835_RALPJ            Unreviewed;       281 AA.
AC   B2U835;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:ACD25877.1};
GN   OrderedLocusNames=Rpic_0726 {ECO:0000313|EMBL:ACD25877.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25877.1};
RN   [1] {ECO:0000313|EMBL:ACD25877.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=12J {ECO:0000313|EMBL:ACD25877.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; CP001068; ACD25877.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2U835; -.
DR   STRING; 402626.Rpic_0726; -.
DR   KEGG; rpi:Rpic_0726; -.
DR   PATRIC; fig|402626.5.peg.1924; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_046120_1_1_4; -.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REPEAT          110..143
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   281 AA;  31289 MW;  D48A3FCDC8AADBDF CRC64;
     MSDITSQNFA QEVIETSRQI PVLVDFWAPW CGPCRTLGPM LEKLEAEFAG KWKLAKINSD
     ENPELSAQFH VRSIPYVVAF VDGKPVDQFV GVLPEAQLRA FLDRVIPQPA EVAYREGLAA
     SQAGETAHAR EAFQNALAFD PGFDAARFAL VNLLLDSGDV HAAQDEFALL SPKAPQDERY
     APLETRLRAT ERADTLPDAG ALRTVVEAQP DNLQARLDLA QQYIAAQDYE AALEQLLAIV
     ERDRAFRDDI ARKTMVSVFD MMRDAPQAVS HWRRQLASKL N
//