ID M7U3Z8_9ARCH Unreviewed; 487 AA. AC M7U3Z8; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 22-FEB-2023, entry version 29. DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:EMR73590.1}; GN ORFNames=MBGDN05_00523 {ECO:0000313|EMBL:EMR73590.1}; OS Thermoplasmatales archaeon SCGC AB-539-N05. OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR73590.1, ECO:0000313|Proteomes:UP000053781}; RN [1] {ECO:0000313|EMBL:EMR73590.1, ECO:0000313|Proteomes:UP000053781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR73590.1}; RX PubMed=23535597; DOI=10.1038/nature12033; RA Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A., RA Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S., RA Schramm A., Jorgensen B.B.; RT "Predominant archaea in marine sediments degrade detrital proteins."; RL Nature 496:215-218(2013). CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EMR73590.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ALXL01000055; EMR73590.1; -; Genomic_DNA. DR AlphaFoldDB; M7U3Z8; -. DR EnsemblBacteria; EMR73590; EMR73590; MBGDN05_00523. DR PATRIC; fig|1198116.5.peg.484; -. DR Proteomes; UP000053781; Unassembled WGS sequence. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR CDD; cd00207; fer2; 1. DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR042204; 2Fe-2S-bd_N. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1. DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1. DR Pfam; PF13510; Fer2_4; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. PE 4: Predicted; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000053781}. FT DOMAIN 117..431 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" SQ SEQUENCE 487 AA; 53118 MW; 65078AD516276E0D CRC64; MVRICKHPIL NFNNRKKISF YFNDKKISGF EGDSIASALC ANDVRVFSHS LKYDRPRGFF CGIGKCSSCL MRVNGIPNVR TCIAPLNDGV RIETQERFAK IPDAKFEDKP KENVDIDILV VGAGPAGLCA SIEAAKQGAN VLLVDENQCV GGQLIKQTHK FFGSKQEKAG TRGIEIAQEL EQKLKTFEGN GSITVMLDST VVGYYEGNRM RYRFGIVKRE GYESRLYEVN CKAVVFSCGA MENMLLFPGN DLPGVYGAGA VQTLMNVYGV KPGKKVIMIG AGNVGLIVSY QLLQAGIKVD RVVEAASTIG GYHVHAAKLR RCGVPIFTSH SIKEIYGDNK VEGAVVVKLD EQWQQIRGSE EKIDCDTICL AVGLTPSIRL LAQVGVKMEF IPEAGGYVAL HDDSMQTTVN KIYVAGDSSG IEEASTAMIE GEIAGVSAAL SLGFDKTAMA LKKQYATQLE NLRAGPFSKK PRVAKRKIEK LLVRQHV //