ID   RURE_PSEOL              Reviewed;         385 AA.
AC   P17052;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Rubredoxin-NAD(+) reductase;
DE            Short=RdxR;
DE            EC=1.18.1.1;
GN   Name=alkT;
OS   Pseudomonas oleovorans.
OG   Plasmid OCT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ALKANE DEGRADATION.
RC   STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX   PubMed=2319593; DOI=10.1016/0022-2836(90)90310-i;
RA   Eggink G., Engel H., Vriend G., Terpstra P., Witholt B.;
RT   "Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to
RT   other flavoprotein oxidoreductases based on one NAD and two FAD
RT   fingerprints.";
RL   J. Mol. Biol. 212:135-142(1990).
RN   [2]
RP   ELECTRON TRANSFER, AND COFACTOR.
RX   PubMed=9799514; DOI=10.1021/bi981853v;
RA   Lee H.J., Basran J., Scrutton N.S.;
RT   "Electron transfer from flavin to iron in the Pseudomonas oleovorans
RT   rubredoxin reductase-rubredoxin electron transfer complex.";
RL   Biochemistry 37:15513-15522(1998).
RN   [3]
RP   INDUCTION.
RX   PubMed=10692156; DOI=10.1046/j.1365-2958.2000.01751.x;
RA   Canosa I., Sanchez-Romero J.M., Yuste L., Rojo F.;
RT   "A positive feedback mechanism controls expression of AlkS, the
RT   transcriptional regulator of the Pseudomonas oleovorans alkane degradation
RT   pathway.";
RL   Mol. Microbiol. 35:791-799(2000).
CC   -!- FUNCTION: Involved in the hydrocarbon hydroxylating system, which
CC       transfers electrons from NADH to rubredoxin reductase and then through
CC       rubredoxin to alkane 1 monooxygenase. {ECO:0000269|PubMed:2319593}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [rubredoxin] = NADH + 2 oxidized
CC         [rubredoxin]; Xref=Rhea:RHEA:18597, Rhea:RHEA-COMP:10302, Rhea:RHEA-
CC         COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.1;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:9799514};
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Induced by AlkS. {ECO:0000269|PubMed:10692156}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ245436; CAB54063.1; -; Genomic_DNA.
DR   PIR; S09114; S09114.
DR   AlphaFoldDB; P17052; -.
DR   SMR; P17052; -.
DR   KEGG; ag:CAB54063; -.
DR   BioCyc; MetaCyc:MON-1021; -.
DR   UniPathway; UPA00191; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015046; F:rubredoxin-NADP+ reductase activity; IDA:UniProtKB.
DR   GO; GO:0043448; P:alkane catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..385
FT                   /note="Rubredoxin-NAD(+) reductase"
FT                   /id="PRO_0000167650"
FT   BINDING         8..11
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         32..33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         156
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         275
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         293
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
SQ   SEQUENCE   385 AA;  41139 MW;  DEF34A08896F91A8 CRC64;
     MAIVVVGAGT AGVNAAFWLR QYGYKGEIRI FSRESVAPYQ RPPLSKAFLT SEIAESAVPL
     KPEGFYTNNN ITISLNTPIV SIDVGRKIVS SKDGKEYAYE KLILATPASA RRLTCEGSEL
     SGVCYLRSME DAKNLRRKLV ESASVVVLGG GVIGLEVASA AVGLGKRVTV IEATPRVMAR
     VVTPAAANLV RARLEAEGIE FKLNAKLTSI KGRNGHVEQC VLESGEEIQA DLIVVGIGAI
     PELELATEAA LEVSNGVVVD DQMCTSDTSI YAIGDCAMAR NPFWGTMVRL ETIHNAVTHA
     QIVASSICGT STPAPTPPRF WSDLKGMALQ GLGALKDYDK LVVAINNETL ELEVLAYKQE
     RLIATETINL PKRQGALAGS IKLPD