ID A0A0B2AQZ2_9MICC Unreviewed; 326 AA.
AC A0A0B2AQZ2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN ORFNames=LK10_05480 {ECO:0000313|EMBL:KHL04362.1};
OS Sinomonas humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL04362.1, ECO:0000313|Proteomes:UP000030982};
RN [1] {ECO:0000313|EMBL:KHL04362.1, ECO:0000313|Proteomes:UP000030982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL04362.1,
RC ECO:0000313|Proteomes:UP000030982};
RA Lee L.-H.;
RT "Genome sequence of Sinomonas sp. MUSC 117.";
RL Submitted (SEP-2014) 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|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:KHL04362.1}.
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DR EMBL; JTDL01000079; KHL04362.1; -; Genomic_DNA.
DR RefSeq; WP_043120786.1; NZ_JTDL01000079.1.
DR AlphaFoldDB; A0A0B2AQZ2; -.
DR STRING; 1338436.LK10_05480; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000030982; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030982}.
FT DOMAIN 13..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 326 AA; 34414 MW; EA2F54966519775A CRC64;
MSTADSNAAE VRDVIVVGSG PAGYTTAIYT ARANLKPLIF AGSVTAGGEL MNTTEVENFP
GFPDGVQGPE LMDKLEQQAA KFGAQIEFED VASVDLEGEV KRVVLGNGEE HLARAVVIAT
GSAYRELGLP NEKRLSGHGV SWCATCDGFF FKDQDIAVIG GGDSAMEEAL FLTKFARSVT
VVHRRDSLRA SKIMADRALA HEKIKFAWNS EVADVRGEDK VTGLVLRSTV DGSESELDVT
GIFVAIGNDP RTELVKGTLA LTPEGTIAVE GRTSRTSIPG VFAAGDVVDP TYRQAITAAG
SGCVAALDVE HYLANLEVPT LATQHA
//
