ID   RURE_ALCBS              Reviewed;         382 AA.
AC   Q0VTB0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Rubredoxin-NAD(+) reductase;
DE            Short=RdxR;
DE            EC=1.18.1.1;
GN   Name=rubB; OrderedLocusNames=ABO_0162;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19953301; DOI=10.1007/s10529-009-0177-0;
RA   Miri M., Bambai B., Tabandeh F., Sadeghizadeh M., Kamali N.;
RT   "Production of a recombinant alkane hydroxylase (AlkB2) from Alcanivorax
RT   borkumensis.";
RL   Biotechnol. Lett. 32:497-502(2010).
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:19953301}.
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:0000269|PubMed:19953301}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AM286690; CAL15610.1; -; Genomic_DNA.
DR   RefSeq; WP_011587459.1; NC_008260.1.
DR   AlphaFoldDB; Q0VTB0; -.
DR   SMR; Q0VTB0; -.
DR   STRING; 393595.ABO_0162; -.
DR   EnsemblBacteria; CAL15610; CAL15610; ABO_0162.
DR   KEGG; abo:ABO_0162; -.
DR   eggNOG; COG1251; Bacteria.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; GIDPGHK; -.
DR   OrthoDB; 1149616at2; -.
DR   BRENDA; 1.18.1.1; 7738.
DR   UniPathway; UPA00191; -.
DR   Proteomes; UP000008871; Chromosome.
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; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR041364; Rbx-bd.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18113; Rbx_binding; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..382
FT                   /note="Rubredoxin-NAD(+) reductase"
FT                   /id="PRO_0000392227"
FT   BINDING         9..12
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         33..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         80
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         287
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT   BINDING         318
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HTK9"
SQ   SEQUENCE   382 AA;  40362 MW;  96D85567B26F84CD CRC64;
     MHPIVIVGTG LAGFNTVKEF RKLDKETPIV MLTADDGRNY SKPMLSAGFS KGKTADDLCM
     ATPEKVAEQL NVDVRTGVHV AGIDATNKRV LLPDDHLDYS KLVLALGADT WTPPLEGDAV
     GEVFSVNDLM DYGKFRAAVE GKKTVTILGG GLIGCEFAND LSNGGFKVSL VEPMGRCLPL
     LLPEQASEAV GRGLADLGVQ FHFGPLAKAV HHGDNGQLVT ELSDGSQLES DVVLSAIGLR
     PRISLAKEAG LDTNRGILTD KSLRTSAEHI YALGDCAEVQ GHVLPYVLPL MASARALAKT
     LAGETTEVSY GVMPVTIKTP ACPVVVCPAA EGSEGAWEVE AEGNTVQALF RSKDGSLLGY
     ALTGEAVKEK MKLNKELPAI MP