ID E5G6W2_9NOCA Unreviewed; 413 AA.
AC E5G6W2; A0A0F6VM77;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:UYF95287.1};
DE SubName: Full=RubR {ECO:0000313|EMBL:ADR72657.1};
GN Name=rubR {ECO:0000313|EMBL:ADR72657.1};
GN ORFNames=OCS65_05870 {ECO:0000313|EMBL:UYF95287.1};
OS Rhodococcus aetherivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=191292 {ECO:0000313|EMBL:ADR72657.1};
RN [1] {ECO:0000313|EMBL:ADR72657.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCP1 {ECO:0000313|EMBL:ADR72657.1};
RX PubMed=21193665; DOI=10.1128/AEM.01987-10;
RA Cappelletti M., Fedi S., Frascari D., Ohtake H., Turner R.J., Zannoni D.;
RT "Analyses of both the alkB Gene Transcriptional Start Site and alkB
RT Promoter-Inducing Properties of Rhodococcus sp. Strain BCP1 Grown on n-
RT Alkanes.";
RL Appl. Environ. Microbiol. 77:1619-1627(2011).
RN [2] {ECO:0000313|EMBL:UYF95287.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N1 {ECO:0000313|EMBL:UYF95287.1};
RA Jiang W.;
RT "The genome sequence of Rhodococcus aetherivorans N1.";
RL Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; HM771649; ADR72657.1; -; Genomic_DNA.
DR EMBL; CP106982; UYF95287.1; -; Genomic_DNA.
DR RefSeq; WP_029546046.1; NZ_JAALEG010000108.1.
DR STRING; 191292.AAT18_22460; -.
DR GeneID; 83619925; -.
DR KEGG; rav:AAT18_22460; -.
DR PATRIC; fig|191292.16.peg.4167; -.
DR HOGENOM; CLU_003291_4_0_11; -.
DR Proteomes; UP001163947; Chromosome.
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 318..401
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 413 AA; 43248 MW; F301A58B8864C4E8 CRC64;
MTETIVVVGT GVAGATAAQT LRKEGFAGRV VLIGEEAALP YRRPVLSKDL LAGSITAERA
QLEPAGYWAD HDIDLRTETR VVELDPRRHR LRLWDNEILD YDAVILATGA RARHLDHDGG
DRVLSLRTAE NVAPLRAAIE AHRSLLVVGA GLIGCEVAST ARELGAEVTV LESAPSPLAR
IVPPAVAEMY VGLHAERDVP VHTGVALRSL TGDDDGVHAT AEDGRAWTAG AALVAVGSVP
DTALARAAGL TVGDGIVVDE AYRTSAAGVY AAGDAIEQPN PVLGGRHRTE NWNSARAQGI
AAAKSVLGQP LGAAEVPWGW SNQYGHNLQF AGWSRHDDDY VVRGSIEGRD FTALALRGDR
LVGAIALGRP KDIRIVRQLV AAGAAVDRGA LADESVALGD VAGRRAAATP ASL
//
