ID   THIO_METTM              Reviewed;          85 AA.
AC   P42035; D9PX45;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Probable Thioredoxin;
DE   AltName: Full=Glutaredoxin-like protein;
GN   OrderedLocusNames=MTBMA_c12030;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-84.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=1587836; DOI=10.1016/s0021-9258(19)50053-9;
RA   McFarlan S.C., Terrell C.A., Hogenkamp H.P.C.;
RT   "The purification, characterization, and primary structure of a small redox
RT   protein from Methanobacterium thermoautotrophicum, an archaebacterium.";
RL   J. Biol. Chem. 267:10561-10569(1992).
CC   -!- FUNCTION: Does not function as a glutathione-disulfide oxidoreductase
CC       in the presence of glutathione and glutathione reductase. May be a
CC       component of a ribonucleotide-reducing system distinct from the
CC       previously described systems utilizing thioredoxin or glutaredoxin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; CP001710; ADL58793.1; -; Genomic_DNA.
DR   RefSeq; WP_013296015.1; NC_014408.1.
DR   AlphaFoldDB; P42035; -.
DR   SMR; P42035; -.
DR   STRING; 79929.MTBMA_c12030; -.
DR   EnsemblBacteria; ADL58793; ADL58793; MTBMA_c12030.
DR   GeneID; 9704911; -.
DR   KEGG; mmg:MTBMA_c12030; -.
DR   PATRIC; fig|79929.8.peg.1169; -.
DR   HOGENOM; CLU_090389_20_2_2; -.
DR   OMA; YGIMAVP; -.
DR   OrthoDB; 110723at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR004502; Thio_glut.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00411; redox_disulf_1; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1587836"
FT   CHAIN           2..85
FT                   /note="Probable Thioredoxin"
FT                   /id="PRO_0000141648"
FT   DOMAIN          2..85
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        13..16
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        62
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9406 MW;  8666A5E87CF502BB CRC64;
     MVVKIEVFTS PTCPYCPMAI EVVDEAKKEF GDKIDVEKID IMVDREKAID YGLMAVPAIA
     INGVVRFVGA PGREELFEAI SDEIE