ID A0A0F0M0Q5_9MICO Unreviewed; 558 AA.
AC A0A0F0M0Q5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KJL37206.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:KJL37206.1};
GN Name=trxB_1 {ECO:0000313|EMBL:KJL37206.1};
GN ORFNames=RR49_01094 {ECO:0000313|EMBL:KJL37206.1};
OS Microbacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL37206.1, ECO:0000313|Proteomes:UP000033451};
RN [1] {ECO:0000313|EMBL:KJL37206.1, ECO:0000313|Proteomes:UP000033451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL37206.1,
RC ECO:0000313|Proteomes:UP000033451};
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 -!- 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:KJL37206.1}.
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DR EMBL; JYIY01000068; KJL37206.1; -; Genomic_DNA.
DR RefSeq; WP_045247056.1; NZ_JYIY01000068.1.
DR AlphaFoldDB; A0A0F0M0Q5; -.
DR STRING; 400772.RR49_01094; -.
DR PATRIC; fig|400772.4.peg.1118; -.
DR OrthoDB; 9786503at2; -.
DR Proteomes; UP000033451; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KJL37206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033451}.
FT DOMAIN 6..285
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 353..447
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 450..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 58111 MW; 74561E0E6BD45FEC CRC64;
MHPDLDVIIL GGGIAGLSAA QLLGRARRRT LVIDAGKPRN RTASHVHGVL GHDGTPPADL
LARGRDEASG YGVGVIEARA VAVEATDDDI TVVTDDGARR TARALLVATG ASDVLPAVAG
LAERWGAGVL HCPYCHGWEV RDRRLGVLAT SPRSLHQAQL VRQWSADVTL FTADLGPLSI
DDDLRLRARG IRLVPQRVVE IVGDGPDVTG VRLADGTMLA LDAVFTGGDL TPHDDVLAGL
DLPRVDSPTG SVIEVDAAGR TAHPRIWAAG NVVTPMASVP MSMAAGATAG AAVNAALVDE
DVARVHADRD RWPEIAPADF WEHRYAASTQ VWSGRVNAVL ADIAATLPAG SALDLGCGEG
GDVLWLAAHG WRATGIDISV TAIGRARAAA ADAGADAASA RFVAGDLAAL DVDETFDLVT
ASFLHSPVDL PREEILRAAA ERVAPGGHLL ITSHAAPPPG SPGAGHGHGH GHDGHHPAPG
HDREGGAPHD HGHGGARHPD PAAPARRWFP TPAEDVAALA LDPAEWTVLI AEERQRESLA
RDGELRTFHD GIVLARRH
//
