ID Q8PUT2_METMA Unreviewed; 76 AA.
AC Q8PUT2;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR037031};
GN OrderedLocusNames=MM_2249 {ECO:0000313|EMBL:AAM31945.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM31945.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM31945.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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: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; AE008384; AAM31945.1; -; Genomic_DNA.
DR RefSeq; WP_011034177.1; NC_003901.1.
DR AlphaFoldDB; Q8PUT2; -.
DR GeneID; 82161315; -.
DR KEGG; mma:MM_2249; -.
DR PATRIC; fig|192952.21.peg.2579; -.
DR eggNOG; arCOG02713; Archaea.
DR HOGENOM; CLU_090389_18_2_2; -.
DR Proteomes; UP000000595; 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 Transport {ECO:0000256|PIRNR:PIRNR037031}.
FT DOMAIN 1..75
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT DISULFID 10..13
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ SEQUENCE 76 AA; 8446 MW; EEF6AF04C50C5A53 CRC64;
MKIEILGTGC PKCKKTKETI EKVLKQTGVE AEVIKVEDIE KIMSYGVMVT PAVVIDGEVK
LAGKVPDEKD VRKWMI
//
