ID A0A1N7J1N9_9BACI Unreviewed; 317 AA.
AC A0A1N7J1N9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|ARBA:ARBA00018719, ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=SAMN05421687_103204 {ECO:0000313|EMBL:SIS43298.1};
OS Salimicrobium flavidum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=570947 {ECO:0000313|EMBL:SIS43298.1, ECO:0000313|Proteomes:UP000187608};
RN [1] {ECO:0000313|EMBL:SIS43298.1, ECO:0000313|Proteomes:UP000187608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23127 {ECO:0000313|EMBL:SIS43298.1,
RC ECO:0000313|Proteomes:UP000187608};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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|ARBA:ARBA00000849,
CC ECO:0000256|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333,
CC ECO:0000256|RuleBase:RU003880}.
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DR EMBL; FTOC01000003; SIS43298.1; -; Genomic_DNA.
DR RefSeq; WP_076557765.1; NZ_FTOC01000003.1.
DR AlphaFoldDB; A0A1N7J1N9; -.
DR STRING; 570947.SAMN05421687_103204; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000187608; 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 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003880}.
FT DOMAIN 7..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 317 AA; 34824 MW; AA627106DB4D717E CRC64;
MSEENIYDVI IVGAGPAGMT AAVYTSRANL STLMIERGIP GGQMANTEDV ENYPGYESIL
GPDLSNKMFS HAKKFGAEYA YGDIKEIIDG KEYKTVKAGK KEYKARSIIL GTGAEYKELG
VPGEKELGGR GVSYCAVCDG AFFRDKELVV VGGGDSAVEE GVYLTRFASK VTVVHRRDEL
RAQKILQDRA FDNEKINFIW NTTVSSINDE NGKVGSVTLY DKEAEEEYEY KTDGTFIYIG
LIPLNSAFRN LGVTNEEGYV ETDERMETNV RGVFAAGDIR DKELRQIVTA TGDGSIAAQS
AQHYIENLME ELEKVGS
//
