THIRX_METTH
ID THIRX_METTH Reviewed; 77 AA.
AC O26981;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Thioredoxin {ECO:0000303|PubMed:11939770};
GN OrderedLocusNames=MTH_895 {ECO:0000312|EMBL:AAB85393.1};
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 {ECO:0000312|EMBL:AAB85393.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H
RC {ECO:0000312|Proteomes:UP000005223};
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).
RN [2] {ECO:0000312|PDB:1ILO}
RP STRUCTURE BY NMR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11939770; DOI=10.1021/bi0115176;
RA Bhattacharyya S., Habibi-Nazhad B., Amegbey G., Slupsky C.M., Yee A.,
RA Arrowsmith C., Wishart D.S.;
RT "Identification of a novel archaebacterial thioredoxin: determination of
RT function through structure.";
RL Biochemistry 41:4760-4770(2002).
CC -!- FUNCTION: Does not function as a glutathione-disulfide oxidoreductase
CC in the presence of glutathione and glutathione reductase. Has low
CC thioredoxin activity in vitro. {ECO:0000269|PubMed:11939770}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85393.1; -; Genomic_DNA.
DR PIR; F69219; F69219.
DR PDB; 1ILO; NMR; -; A=1-77.
DR PDBsum; 1ILO; -.
DR AlphaFoldDB; O26981; -.
DR BMRB; O26981; -.
DR SMR; O26981; -.
DR STRING; 187420.MTH_895; -.
DR DNASU; 1471303; -.
DR EnsemblBacteria; AAB85393; AAB85393; MTH_895.
DR KEGG; mth:MTH_895; -.
DR HOGENOM; CLU_090389_18_2_2; -.
DR OMA; DYGVMIT; -.
DR EvolutionaryTrace; O26981; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA: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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..77
FT /note="Thioredoxin"
FT /id="PRO_0000431069"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0AA25"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0AA25"
FT DISULFID 11..14
FT /note="Redox-active"
FT /evidence="ECO:0000303|PubMed:11939770"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1ILO"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1ILO"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1ILO"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1ILO"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1ILO"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1ILO"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1ILO"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1ILO"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1ILO"
SQ SEQUENCE 77 AA; 8455 MW; 7CF7E5B217683B7A CRC64;
MMKIQIYGTG CANCQMLEKN AREAVKELGI DAEFEKIKEM DQILEAGLTA LPGLAVDGEL
KIMGRVASKE EIKKILS
