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Database: UniProt
Entry: A0A0F0L556_9MICO
LinkDB: A0A0F0L556_9MICO
Original site: A0A0F0L556_9MICO 
ID   A0A0F0L556_9MICO        Unreviewed;        61 AA.
AC   A0A0F0L556;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KJL28297.1};
DE            EC=1.8.1.9 {ECO:0000313|EMBL:KJL28297.1};
GN   Name=trxB_5 {ECO:0000313|EMBL:KJL28297.1};
GN   ORFNames=RS83_03368 {ECO:0000313|EMBL:KJL28297.1};
OS   Microbacterium oxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL28297.1, ECO:0000313|Proteomes:UP000033640};
RN   [1] {ECO:0000313|EMBL:KJL28297.1, ECO:0000313|Proteomes:UP000033640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEL4b {ECO:0000313|EMBL:KJL28297.1,
RC   ECO:0000313|Proteomes:UP000033640};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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   -!- 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:KJL28297.1}.
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DR   EMBL; JYIW01000026; KJL28297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0L556; -.
DR   PATRIC; fig|82380.11.peg.3398; -.
DR   Proteomes; UP000033640; Unassembled WGS sequence.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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   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; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KJL28297.1}.
FT   DOMAIN          7..56
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   61 AA;  6025 MW;  94EFEB05922AA7B4 CRC64;
     MSIQEVELVI IGSGPAGYTA AVYAARAGLA PVVLAGSVTA GGALMTTTEV ENFPGFVNGV
     Q
//
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