ID N0BKV2_9EURY Unreviewed; 77 AA.
AC N0BKV2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR037031};
GN ORFNames=Asulf_00831 {ECO:0000313|EMBL:AGK60840.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK60840.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK60840.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK60840.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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; CP005290; AGK60840.1; -; Genomic_DNA.
DR RefSeq; WP_015590438.1; NC_021169.1.
DR AlphaFoldDB; N0BKV2; -.
DR STRING; 387631.Asulf_00831; -.
DR GeneID; 15392472; -.
DR KEGG; ast:Asulf_00831; -.
DR eggNOG; arCOG02713; Archaea.
DR HOGENOM; CLU_090389_18_2_2; -.
DR OrthoDB; 50016at2157; -.
DR Proteomes; UP000013307; 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:UP000013307};
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 77 AA; 8584 MW; F8F0969F2C04E265 CRC64;
MKIKVLGPGC PRCKATYEVV KKVVEKERTD ADIEYVTDMS EATKFGVLVT PAVWVDGEIV
IQGKIPSESE ILKFIKK
//
