ID F2KS41_ARCVS Unreviewed; 300 AA.
AC F2KS41;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:AEA47980.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:AEA47980.1};
GN OrderedLocusNames=Arcve_1987 {ECO:0000313|EMBL:AEA47980.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA47980.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA47980.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002588; AEA47980.1; -; Genomic_DNA.
DR RefSeq; WP_013684632.1; NC_015320.1.
DR AlphaFoldDB; F2KS41; -.
DR STRING; 693661.Arcve_1987; -.
DR GeneID; 10395119; -.
DR KEGG; ave:Arcve_1987; -.
DR eggNOG; arCOG01296; Archaea.
DR HOGENOM; CLU_031864_5_3_2; -.
DR OrthoDB; 27340at2157; -.
DR Proteomes; UP000008136; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEA47980.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000008136}.
FT DOMAIN 3..285
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 300 AA; 32827 MW; ED7682D47D9D2DCE CRC64;
MEYDVAIIGA GPAGLTAAIY AGRYGLRTVF FESMPSQLAV VPFIENYPGF EGSGYELLEK
MKEQATKFAE HRFESVEELK KDGDIFVVKT DSGEYRVKAV IVATGGKHKE LGVPGEKEFV
GRGVSYCATC DGHFFRGKRV LVIGGGNTAV TDAVYLKEIG CDVTLVHRRD ALRADRALQD
ELFKRNIPVI WNSVVERIEG SNRVERVVLL DRVKNEKFVV EADGVFIAVG IRPQTEIVVN
LGVERDSKGY IKVDRRQATS VPGVFAAGDC CDNPLKQVVT ACSDGAIAAN SAFEYIMSKS
//
