ID   THIRX_METJA             Reviewed;          86 AA.
AC   Q58001;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Thioredoxin {ECO:0000250|UniProtKB:O26981};
GN   OrderedLocusNames=MJ0581;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Does not function as a glutathione-disulfide oxidoreductase
CC       in the presence of glutathione and glutathione reductase (By
CC       similarity). Has low thioredoxin activity in vitro (By similarity).
CC       {ECO:0000250|UniProtKB:O26981}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98575.1; -; Genomic_DNA.
DR   PIR; E64372; E64372.
DR   AlphaFoldDB; Q58001; -.
DR   SMR; Q58001; -.
DR   STRING; 243232.MJ_0581; -.
DR   EnsemblBacteria; AAB98575; AAB98575; MJ_0581.
DR   KEGG; mja:MJ_0581; -.
DR   eggNOG; arCOG02713; Archaea.
DR   HOGENOM; CLU_090389_18_1_2; -.
DR   InParanoid; Q58001; -.
DR   OMA; KYGVMST; -.
DR   PhylomeDB; Q58001; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR   InterPro; IPR005243; Redox_disulphide_2.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR36450; PTHR36450; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00412; redox_disulf_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..86
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000141653"
FT   ACT_SITE        15
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AA25"
FT   ACT_SITE        18
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AA25"
FT   DISULFID        15..18
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:O26981"
SQ   SEQUENCE   86 AA;  9634 MW;  AA89FE52EC6C0D67 CRC64;
     MVRVMVVIRI FGTGCPKCNQ TYENVKKAVE ELGIDAEIVK VTDVNEIAEW VFVTPGVAFD
     DVIVFEGKIP SVEEIKEELK SYLEGK