RURE_ACIAD
ID RURE_ACIAD Reviewed; 393 AA.
AC P42454; Q6FDA6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Rubredoxin-NAD(+) reductase;
DE Short=RdxR;
DE EC=1.18.1.1;
GN Name=rubB; OrderedLocusNames=ACIAD1065;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7670642; DOI=10.1099/13500872-141-6-1425;
RA Geissdoerfer W., Frosch C.S., Haspel G., Ehrt S., Hillen W.;
RT "Two genes encoding proteins with similarities to rubredoxin and rubredoxin
RT reductase are required for conversion of dodecane to lauric acid in
RT Acinetobacter calcoaceticus ADP1.";
RL Microbiology 141:1425-1432(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-392.
RA Kok R.G., Bart A., Hellingwerf K.J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN ALKANE DEGRADATION, AND INDUCTION.
RX PubMed=10400587; DOI=10.1128/jb.181.14.4292-4298.1999;
RA Geissdorfer W., Kok R.G., Ratajczak A., Hellingwerf K.J., Hillen W.;
RT "The genes rubA and rubB for alkane degradation in Acinetobacter sp. strain
RT ADP1 are in an operon with estB, encoding an esterase, and oxyR.";
RL J. Bacteriol. 181:4292-4298(1999).
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:10400587}.
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.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:10400587}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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; Z46863; CAA86926.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG67953.1; -; Genomic_DNA.
DR EMBL; X88895; CAA61350.1; -; Genomic_DNA.
DR RefSeq; WP_004921642.1; NC_005966.1.
DR AlphaFoldDB; P42454; -.
DR SMR; P42454; -.
DR STRING; 62977.ACIAD1065; -.
DR EnsemblBacteria; CAG67953; CAG67953; ACIAD1065.
DR GeneID; 45233507; -.
DR KEGG; aci:ACIAD1065; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; GIDPGHK; -.
DR OrthoDB; 1149616at2; -.
DR BioCyc; ASP62977:ACIAD_RS04910-MON; -.
DR UniPathway; UPA00191; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0043448; P:alkane catabolic process; IMP:UniProtKB.
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; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..393
FT /note="Rubredoxin-NAD(+) reductase"
FT /id="PRO_0000167649"
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 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT BINDING 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HTK9"
FT CONFLICT 75..77
FT /note="LSE -> SSD (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..204
FT /note="NLEESG -> IWRKR (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 42464 MW; 2A126C8FC3AB1DA2 CRC64;
MHPIVIIGSG MAGYTLAREF RKLNPEHELV MICADDAVNY AKPTLSNALS GNKAPEQIPL
GDAEKMSTQL KLQILSETWV KAINPETHEL KLEKNGQETI QPYSKLVLAV GANPTRLAIA
GDGSDDIHVV NSLIDYRAFR ENLAKRQDKR VVILGAGLIG CEFANDLQHT GHQVTVIDLS
PRPLGRLLPA HIADAFQKNL EESGIHFVLS TTVEKVSKIN DGQDYAVTLA NGQTLVADIV
LSAIGLQPNI DLAKHAGVHT SRGILTNSLL ETNLEDIYAI GDCAEVNGTL LPYVMPIMQQ
ARALAKTLSG ETTHVHYPAM PVAVKTPAAP LTVLPVPVDV DVNWETEEFE DGMLAKAIDN
TDTLRGFVLL GATAGKQRLT LTKLVPDLIP AQL
