ID   A0A0Q9CBC5_9CELL        Unreviewed;       316 AA.
AC   A0A0Q9CBC5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KRD40540.1};
GN   ORFNames=ASE27_04920 {ECO:0000313|EMBL:KRD40540.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40540.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD40540.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40540.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD40540.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40540.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KRD40540.1}.
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DR   EMBL; LMJG01000011; KRD40540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9CBC5; -.
DR   Proteomes; UP000051694; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 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   Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT   DOMAIN          1..285
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   316 AA;  32150 MW;  FAE81079F247EFDF CRC64;
     MVVGGGAAGL SGALTLARAR RSVLVIDAGR PRNAPAAHMH GYLSRDGEDP AALLATGRAE
     VAAYGGRISQ GTVESATALP DGGFEVLTTD GRAVRARRLL VTTGLVDELP DVPGLAERWG
     KDVLHCPYCH GWEVRDQAVG ILATGPMSIH QAQMWRQWTD DVTLFLHGSP APDAGTRAAL
     DARGIRVVEG RVAGLALDAD ALSGARLASG EVVECTALVV APRFTARSAV LTSLGVETED
     QVVDGVTIGT FAPSDPQGAT SVPGVRVAGN VTNIMAQVVA AAAAGVQAAA ATNGDLIAEE
     VQQALAARAA PSAHAG
//