ID A0A1X0UDM8_9NOCA Unreviewed; 304 AA.
AC A0A1X0UDM8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ORI16276.1};
GN ORFNames=BJI47_14875 {ECO:0000313|EMBL:ORI16276.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI16276.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI16276.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI16276.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
RL Submitted (OCT-2016) 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:ORI16276.1}.
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DR EMBL; MKKY01000079; ORI16276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0UDM8; -.
DR OrthoDB; 9786503at2; -.
DR Proteomes; UP000192546; 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; 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:UP000192546}.
FT DOMAIN 2..273
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 304 AA; 31431 MW; B2FC18B0BAF0B291 CRC64;
MYDVVIVGAG ASGLSAALVL GRQKRSVLVI DGGKPRNAPA AEMHMYLGRD GGVPAQLLAD
GRAEIDAYPT VERVAGQVSA VGGVDGAFEV TIGDGAPLQA HKLFFATGVT DVPWEIPGLA
ELWGSGVFHC PFCHGFETDG LTLGVLANGS NAVLAAYVAD RFSDDVVVCT DGPSTIPDPL
RAMLDKVGAQ VVETPVTHIE GELGSLTVHF ADGSVLERQA LYHRAPTTPN TTLTRTLGCE
HFDDGCVRVD EFGKTTVPGV SAGGDAAHLA AVPEPVTLVA SAAADGVRAA VWLEQDLFSE
AFAS
//
