ID   A0A0G4GMW4_VITBC        Unreviewed;       655 AA.
AC   A0A0G4GMW4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Thioredoxin reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Vbra_465 {ECO:0000313|EMBL:CEM31551.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM31551.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM31551.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; CDMY01000725; CEM31551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4GMW4; -.
DR   STRING; 1169540.A0A0G4GMW4; -.
DR   VEuPathDB; CryptoDB:Vbra_465; -.
DR   InParanoid; A0A0G4GMW4; -.
DR   OrthoDB; 5473641at2759; -.
DR   PhylomeDB; A0A0G4GMW4; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR   NCBIfam; TIGR01438; TGR; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..655
FT                   /note="Thioredoxin reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005190705"
FT   DOMAIN          117..463
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          573..630
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   655 AA;  69167 MW;  CC2FC4B250EB935C CRC64;
     MAPIAILAAI LFCNVAASNV EEMAAGHEAH VTNNKSTCPH SFVEDTQTLA KAKHPTSKES
     DVVSDEVQGA VIGGIIGGKN GSAGAVGGAM HGTGGAMYGG LMGSSGTATS AAPLSRYDLV
     VIGGGSGGMA AAKEAAKLGK RVALFDYPSP QGTTWGIGGT CLNVGCIPRK LMHYAALIGA
     SFYDARLLGW QLPDVRGQGH SGIAHDWGQL VKFVRNKVRQ LRFSYGNALR SYGNSLTYVN
     ALARFESAGV IEYENPSSGE TQKLTADKVL IAVGGRPNIP EDIPGAVEHD ITSDDIFTLD
     RPPGRTLVVG AGYIALETAG FLNEINFDVS VAVRSVVLRG FDRQCAEKIA QLMAEVGVRF
     MYSVTVGSIT KKQPDESGLP SLEVELRSRD GNIVTEVYNT VLFATGRTPE TASLGLDAVG
     VKYDAQTSKI AVNDVEQTSV PNVYAVGDCI PQLELTPVAV RAGEVLARRL YGGSTEKMDY
     EMVPTTVFTP FEYGSVGLSE EQAVKKYGKD AIETFLLEVE TAHTDPPALS RLAHSSAPLL
     THFEDLELSG VHRPKVATAR SDGFDIFLSA SNLSKLVCLR NENNRVVGFH YVGRNAGEVT
     QGFALALRLG ATKSDFDRML GIQPTDAESF SGLTVTRRSG ESFVAAGGCG GGRCG
//