ID Q8VQU3_9NOCA Unreviewed; 412 AA.
AC Q8VQU3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=Reductase {ECO:0000313|EMBL:AAL61666.1};
OS Rhodococcus aetherivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=191292 {ECO:0000313|EMBL:AAL61666.1};
RN [1] {ECO:0000313|EMBL:AAL61666.1}
RP NUCLEOTIDE SEQUENCE OF 55-412.
RC STRAIN=I24 {ECO:0000313|EMBL:AAL61666.1};
RA Fonstein M.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAL61666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I24 {ECO:0000313|EMBL:AAL61666.1};
RX PubMed=15069586; DOI=10.1007/s00253-004-1589-3;
RA Priefert H., O'Brien X.M., Lessard P.A., Dexter A.F., Choi E.E., Tomic S.,
RA Nagpal G., Cho J.J., Agosto M., Yang L., Treadway S.L., Tamashiro L.,
RA Wallace M., Sinskey A.J.;
RT "Indene bioconversion by a toluene inducible dioxygenase of Rhodococcus sp.
RT I24.";
RL Appl. Microbiol. Biotechnol. 65:168-176(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF452376; AAL61666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VQU3; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
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 InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 4..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..401
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 412 AA; 43471 MW; BE0A64798348C1C4 CRC64;
MTSDIVVIGG GVAGVSAVQS LRSEGYDGRL FLIGKERELP YDRTSLSKAV LAGDLADPPP
LSPADWYDEL QVETVLDRTV LQVDVTRKEV LLDGGRSLEV DRVLLATGAS ARVPSFSGAD
LPGVTTLRTV DDAQRLRQDW EPGQRLVVVG GGLIGCEVAT TARKLGLEVS ILEASDELLQ
RVLGRRIGGW CRARLEELGI SVMVNTGVAE FDGVDRITAV IGTDGRRFPA DSAIVCVGAE
PETAIAEQAG LACSRGIIVN DSGGTAAEGV FAAGDAASWP LRTGGRRSLE TYINSQKEAT
AVASAMLGKA VHAPQLPLSW TEIAGHRIQM IGDIEGSGEY VMRGAPDDGP ALLFRLTDGK
LTAALSVDAP REFAMATRLV ESGAQVGRDV LADTSVELRE LNRAARERTT AA
//
