ID A0A0K1JL91_9MICO Unreviewed; 566 AA.
AC A0A0K1JL91;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:AKU17494.1};
GN ORFNames=VV02_19355 {ECO:0000313|EMBL:AKU17494.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17494.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU17494.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17494.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-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};
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DR EMBL; CP011112; AKU17494.1; -; Genomic_DNA.
DR RefSeq; WP_052594165.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JL91; -.
DR STRING; 571913.VV02_19355; -.
DR KEGG; lmoi:VV02_19355; -.
DR PATRIC; fig|571913.6.peg.3919; -.
DR OrthoDB; 109585at2; -.
DR Proteomes; UP000066480; Chromosome.
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:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000066480}.
FT DOMAIN 237..542
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 566 AA; 59442 MW; B69AC65E034F77D6 CRC64;
MKPATPAILL VTSDHRDEVV DEVNSRYARD YDVVVAGGLG EAVAAASSMQ SRDVPVALIA
VERSLPDAQG LVTIDCLHAL IPTAKRLLLT AWEDWATAKE EIQQAQTTGR LDVSLVIPRG
ARDEEFHTAI TESLSDWGWT TGGPVVDVVR IVSDQETSEL NAMRDFLDRM GVPTRVYPSA
SPAAKEVLAR AVSAGRPTDL PLVAAFDHDP ISRPSIGKLG RVMFGDPDAL GEDYVADLAV
VGAGPAGLAA AVYGASEGLA TVVLDSEAIG GQAGTSSMIR NYLGFPRGIS GMRLAQRARF
QASRFGARFF AARPVTSVVP GVDGAPHLIQ LEGFTIRART IVIASGVSYR RLGVPAIEDL
VGLGVNYGAA MSAARDCAGT DVFVVGGGNS AGQAAIHLSR FARSVSILIR RDSLTETMSD
YLIREIEGNS RIVVRPQTEV VDGGGGTRLE WLKLKGVGGE ITKVHAGGLF LLLGAKPCVD
WIPDTVALDE RGFVRTGRDV PQDQWGGDVP PEALATTVPG VFAAGDVRSG SMKRVASASG
EGAAVVPLVH TYLDESAPVP VVVPSA
//
