THIO_METTH
ID THIO_METTH Reviewed; 85 AA.
AC O26898;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Probable Thioredoxin;
DE AltName: Full=Glutaredoxin-like protein;
GN OrderedLocusNames=MTH_807;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Acts to maintain redox homeostasis; functions as a protein
CC disulfide reductase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85307.1; -; Genomic_DNA.
DR PIR; G69207; G69207.
DR RefSeq; WP_010876442.1; NC_000916.1.
DR PDB; 1NHO; NMR; -; A=1-85.
DR PDBsum; 1NHO; -.
DR AlphaFoldDB; O26898; -.
DR BMRB; O26898; -.
DR SMR; O26898; -.
DR STRING; 187420.MTH_807; -.
DR EnsemblBacteria; AAB85307; AAB85307; MTH_807.
DR GeneID; 24853940; -.
DR KEGG; mth:MTH_807; -.
DR PATRIC; fig|187420.15.peg.792; -.
DR HOGENOM; CLU_090389_20_2_2; -.
DR OMA; YGIMAVP; -.
DR EvolutionaryTrace; O26898; -.
DR Proteomes; UP000005223; 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 3D-structure; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..85
FT /note="Probable Thioredoxin"
FT /id="PRO_0000141647"
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 STRAND 5..9
FT /evidence="ECO:0007829|PDB:1NHO"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1NHO"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1NHO"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1NHO"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1NHO"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1NHO"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1NHO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1NHO"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1NHO"
SQ SEQUENCE 85 AA; 9481 MW; 8666D5EF70BEF00B CRC64;
MVVNIEVFTS PTCPYCPMAI EVVDEAKKEF GDKIDVEKID IMVDREKAIE YGLMAVPAIA
INGVVRFVGA PSREELFEAI NDEME