ID A0A0Q5LHE7_9MICO Unreviewed; 567 AA.
AC A0A0Q5LHE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Thioredoxin reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF82_07145 {ECO:0000313|EMBL:KQR47395.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR47395.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR47395.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47395.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR47395.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47395.1,
RC ECO:0000313|Proteomes:UP000051005};
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:KQR47395.1}.
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DR EMBL; LMOX01000001; KQR47395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5LHE7; -.
DR STRING; 1736282.ASF82_07145; -.
DR Proteomes; UP000051005; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR Pfam; PF13649; Methyltransf_25; 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 SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051005}.
FT DOMAIN 4..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 401..496
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 567 AA; 59025 MW; 16D6A60167448E12 CRC64;
MVRDVLVVGG GAAGLSAGLT LARARRDVVV VDAGEPRNAP AAGVHGFLTR DGIAPAELTR
LGRAEVESHG GEVGAGTVTA LDRVEPAPGV AARFRASVTH AGGRVETVLA RRVVVTTGVS
DQLPPMAGLA ERWGRDAVHC PYCHGWEVRD RLIGVLGGGP LSVHQALLFR QWSDRVVLFL
NDALEPTEEE WEQLAARGIG VVTGAVTRVL VTDDRMSGVE LASGRTRPVE ALALGAALRV
NSDLLTGLGV EQEPHPLGVG LVVPSDPATG ATSVPGLWLA GNVADPMMQV VAAAASGVRA
AALANADLVA EDTALAVAAR RAPFSAAAES AGTARLLGER RYGVAPRSGD ADGPAPGRPE
QEVFDRAYWE ERYGSEGFTW SGEPNAQLVA ETVDLTPGRA LDVGSGEGGD AIWLARRGWT
VTGTDIAEAA LAKAARRAEA TDPAAAARIT WEQHDVTTWA PEPGAFDLVS AQFMHLADPE
RAVLFRGLAA AVAPGGTLLV VGHDLTDDPE RMAHRRDLMF TVDDVLAAIE GEGLEVEVAG
SRERAATSAH HGGGPMRDVV VRAHRAS
//
