ID   RURE_PSEPU              Reviewed;         385 AA.
AC   Q9L4M8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Rubredoxin-NAD(+) reductase;
DE            Short=RdxR;
DE            EC=1.18.1.1;
GN   Name=alkT;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1;
RX   PubMed=11207749; DOI=10.1046/j.1462-2920.1999.00037.x;
RA   Smits T.H.M., Roethlisberger M., Witholt B., Van Beilen J.B.;
RT   "Molecular screening for alkane hydroxylase genes in Gram-negative and
RT   Gram-positive strains.";
RL   Environ. Microbiol. 1:307-317(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1;
RX   PubMed=11390693; DOI=10.1099/00221287-147-6-1621;
RA   Van Beilen J.B., Panke S., Lucchini S., Franchini A.G., Roethlisberger M.,
RA   Witholt B.;
RT   "Analysis of Pseudomonas putida alkane degradation gene clusters and
RT   flanking insertion sequences: evolution and regulation of the alk-genes.";
RL   Microbiology 147:1621-1630(2001).
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:0000250}.
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; Evidence={ECO:0000305};
CC   -!- PATHWAY: Hydrocarbon metabolism; alkane degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ233397; CAB69078.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L4M8; -.
DR   SMR; Q9L4M8; -.
DR   UniPathway; UPA00191; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR   GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015046; F:rubredoxin-NADP+ reductase activity; ISS: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; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..385
FT                   /note="Rubredoxin-NAD(+) reductase"
FT                   /id="PRO_0000392228"
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;  40956 MW;  9DC4DE35E3C3CCA8 CRC64;
     MAIVIVGAGT AGVNAAFWLR QYGYKGGIRL LSRESVTPYQ RPPLSKAFLT SETAESAIPL
     KPESFYTNNN ISISLNTQIV SIDVGRKVVA AKDGEEYAYE KLILATGASA RRLTCEGSEL
     SGVCYLRSME DAKNLRRKLV ESASVVVLGG GVIGLEVASA AVGIGRRVTV IEAAPRVMAR
     VVTPAAANLV RARLEAEGVG FKLNAKLTSI KGRNGHVNQC VLESGEKIQA DLIIVGIGAI
     PELELATEAA LEVSNGVVVD DQMRTSDTSI YAIGDCALAR NLFFGTMVRL ETIHNAVTQA
     QIVASSICGT STPAPTPPRF WSDLKGMTLQ GLGALKDYDK LVVAINNETV ELEVLAYKQE
     RLIATETINL PKRQGALGGS IKLPD