ID A0A175RYK6_9MICO Unreviewed; 343 AA.
AC A0A175RYK6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KTR08836.1};
GN ORFNames=NS184_04780 {ECO:0000313|EMBL:KTR08836.1};
OS Curtobacterium luteum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=33881 {ECO:0000313|EMBL:KTR08836.1, ECO:0000313|Proteomes:UP000078252};
RN [1] {ECO:0000313|EMBL:KTR08836.1, ECO:0000313|Proteomes:UP000078252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS184 {ECO:0000313|EMBL:KTR08836.1,
RC ECO:0000313|Proteomes:UP000078252};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR08836.1}.
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DR EMBL; LDQC01000026; KTR08836.1; -; Genomic_DNA.
DR RefSeq; WP_058724995.1; NZ_LDQC01000026.1.
DR AlphaFoldDB; A0A175RYK6; -.
DR STRING; 33881.NS184_04780; -.
DR PATRIC; fig|33881.3.peg.1230; -.
DR OrthoDB; 9786503at2; -.
DR Proteomes; UP000078252; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 323..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 34441 MW; D072652CC6E114D3 CRC64;
MRDHFDVIVI GGAAAGLSAA LILGRSRRSV LVVDAGEPRN APADGIHNYL GREGASPSEL
GRVGREEVAS YGVEVTTGRI VATSATDGDG TDPVGFSVTL DSAAVVTARR LVVASGAVDV
LPEVPGLAEQ WGRGVVHCPF CHGWEIRDHR IGVLVTTPNG AHHALMFRAL SDDVTAFVTD
PVLLDDTTLA GLRARGIRVM PGPVTAVDSE DDRLTGVALG SGEFVALDAL AAASTVEARV
DFLAGVGLEA TDFIVGGHRF GSALTVDGAG QTSVRGVYAA GNVTVPMATV IASAAAGTAV
GAAVHGDLVQ ADLAAAVATA ASSASSASAS SSSSGSSPLQ STR
//
