ID   M0FKH8_9EURY            Unreviewed;       349 AA.
AC   M0FKH8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:ELZ59838.1};
GN   ORFNames=C460_05511 {ECO:0000313|EMBL:ELZ59838.1};
OS   Haloferax sp. ATCC BAA-646.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1227464 {ECO:0000313|EMBL:ELZ59838.1, ECO:0000313|Proteomes:UP000011677};
RN   [1] {ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|Proteomes:UP000011677};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELZ59838.1, ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|EMBL:ELZ59838.1,
RC   ECO:0000313|Proteomes:UP000011677};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:ELZ59838.1}.
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DR   EMBL; AOLD01000019; ELZ59838.1; -; Genomic_DNA.
DR   RefSeq; WP_008573712.1; NZ_AOLD01000019.1.
DR   AlphaFoldDB; M0FKH8; -.
DR   PATRIC; fig|1227464.4.peg.1080; -.
DR   Proteomes; UP000011677; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
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   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   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          13..322
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   349 AA;  37257 MW;  30278B95CB656D6A CRC64;
     MTEDADSFVE HRKLIIAGSG ISGLSSAIYA ARSNNEPLVL EGDEPGGQLT LTTEVDNYPG
     FPEGISGPEL INNMKEQAER FGTEIRHGII EDVDASERPF TVTLKNGDVY TADALIAASG
     ASARTLGIPG EENLMGYGLS TCATCDGAFF RGEKIMVIGG GDAAVEEANF LTKFASTVYL
     VHRREEFRAE DYWVDRLMEK VDEGEIELML NTEATELHGS PEEGVDHVTL VRNPEGHPSD
     KLDDPGTEEF DFDVGAVFYA IGHTPNADYL EGTGVQRDDD GYIVAKGGSG GGQTATDVPG
     IFAAGDVVDY HYQQAATAGG MGVKAALDAD DYLEELEREE KRAAAGAAE
//