ID A0A1E2WUX9_9NOSO Unreviewed; 456 AA.
AC A0A1E2WUX9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=A4S05_27505 {ECO:0000313|EMBL:ODH01783.1};
OS Nostoc sp. KVJ20.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=457944 {ECO:0000313|EMBL:ODH01783.1, ECO:0000313|Proteomes:UP000094607};
RN [1] {ECO:0000313|EMBL:ODH01783.1, ECO:0000313|Proteomes:UP000094607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KVJ20 {ECO:0000313|EMBL:ODH01783.1,
RC ECO:0000313|Proteomes:UP000094607};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003880};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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:ODH01783.1}.
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DR EMBL; LSSA01000055; ODH01783.1; -; Genomic_DNA.
DR RefSeq; WP_069072963.1; NZ_KV757675.1.
DR AlphaFoldDB; A0A1E2WUX9; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000094607; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR CDD; cd02949; TRX_NTR; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF26; NADPH-DEPENDENT THIOREDOXIN REDUCTASE 3; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|RuleBase:RU003880}.
FT DOMAIN 339..456
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 331..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 49759 MW; FD50F5D9081F2344 CRC64;
MTNPTVENLV IIGSGPAGYT AAIYAGRANL KPVVFEGFQA GGLPGGQLMT TTEVENFPGF
PKGITGPELM DQMKAQAERW GAELYTEDVI SVDLSQRPFT VRSQEREIKT NSIVIATGAT
AKRLGLPSEH EFWSRGISAC AICDGATPIF HGAELAVIGA GDSAAEESIY LTKYGSKVNM
LVRTDKMRAS KAMQDRVLSN PKIQVHWNTE AVDIFGSDRM EGVKVRNTKT GEESKLDAKG
LFYAVGHTPN TSLFKGQLEL DEVGYVVTKH GTVETSVEGV FAAGDVQDHE FRQAITAAGT
GCMAAMLAER WLSSSGLIQE FHQQLETADN ELENQPAKKT EAEEEAGFNL DGTRHEGGYA
LRKLFHESDR LLLVKYVSPG CGPCHTLKPI LNKVVDEFDS KIHFVEIDID KDRDIAENAG
VTGTPTVQLF KNKELVKEVK GVKQKSEYRQ LIESSL
//
