ID I7KAM9_METBM Unreviewed; 80 AA.
AC I7KAM9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR037031};
GN OrderedLocusNames=BN140_0013 {ECO:0000313|EMBL:CCJ34936.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ34936.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
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:0000256|PIRNR:PIRNR037031}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {ECO:0000256|ARBA:ARBA00007787, ECO:0000256|PIRNR:PIRNR037031}.
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DR EMBL; HE964772; CCJ34936.1; -; Genomic_DNA.
DR RefSeq; WP_014865913.1; NC_018227.2.
DR AlphaFoldDB; I7KAM9; -.
DR STRING; 1201294.BN140_0013; -.
DR GeneID; 13355309; -.
DR KEGG; mbg:BN140_0013; -.
DR PATRIC; fig|1201294.9.peg.14; -.
DR HOGENOM; CLU_090389_18_2_2; -.
DR BioCyc; MBOU1201294:BN140_RS00060-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR005243; THIRX-like_proc.
DR NCBIfam; TIGR00412; redox_disulf_2; 1.
DR PANTHER; PTHR36450; THIOREDOXIN; 1.
DR PANTHER; PTHR36450:SF1; THIOREDOXIN; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037031-51};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR037031};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR037031,
KW ECO:0000256|PIRSR:PIRSR037031-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007};
KW Transport {ECO:0000256|PIRNR:PIRNR037031}.
FT DOMAIN 2..76
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT DISULFID 11..14
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ SEQUENCE 80 AA; 8575 MW; 493088FACC784473 CRC64;
MVKIEVLGTG CAKCRRLAKN VESAINDLGI DAEVVKVDDI TEIMDRGVML TPALAVDGEL
KVSGRVADVR EIKEILHGAD
//
