P42454 (RURE_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rubredoxin-NAD(+) reductase
Short name=RdxR
EC=1.18.1.1

Gene names

Name:	rubB
Ordered Locus Names:	ACIAD1065

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. Ref.4
Catalytic activity	2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH.
Cofactor	FAD Potential.
Pathway	Hydrocarbon metabolism; alkane degradation.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Induction	Constitutively expressed. Ref.4
Sequence similarities	Belongs to the FAD-dependent oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alkane catabolic process Inferred from mutant phenotype Ref.4. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro rubredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Rubredoxin-NAD(+) reductase		PRO_0000167649
Regions
	Nucleotide binding	9 – 12	4	FAD or NAD By similarity
	Nucleotide binding	33 – 34	2	FAD or NAD By similarity
	Nucleotide binding	282 – 294	13	FAD or NAD By similarity
Sites
	Binding site	42	1	FAD or NAD By similarity
	Binding site	80	1	FAD or NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	162	1	FAD or NAD By similarity
	Binding site	325	1	FAD or NAD By similarity
Experimental info
	Sequence conflict	75 – 77	3	LSE → SSD Ref.1
	Sequence conflict	199 – 204	6	NLEESG → IWRKR Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42454 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: 2A126C8FC3AB1DA2	FASTA	393	42,464
	10 20 30 40 50 60 MHPIVIIGSG MAGYTLAREF RKLNPEHELV MICADDAVNY AKPTLSNALS GNKAPEQIPL 70 80 90 100 110 120 GDAEKMSTQL KLQILSETWV KAINPETHEL KLEKNGQETI QPYSKLVLAV GANPTRLAIA 130 140 150 160 170 180 GDGSDDIHVV NSLIDYRAFR ENLAKRQDKR VVILGAGLIG CEFANDLQHT GHQVTVIDLS 190 200 210 220 230 240 PRPLGRLLPA HIADAFQKNL EESGIHFVLS TTVEKVSKIN DGQDYAVTLA NGQTLVADIV 250 260 270 280 290 300 LSAIGLQPNI DLAKHAGVHT SRGILTNSLL ETNLEDIYAI GDCAEVNGTL LPYVMPIMQQ 310 320 330 340 350 360 ARALAKTLSG ETTHVHYPAM PVAVKTPAAP LTVLPVPVDV DVNWETEEFE DGMLAKAIDN 370 380 390 TDTLRGFVLL GATAGKQRLT LTKLVPDLIP AQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two genes encoding proteins with similarities to rubredoxin and rubredoxin reductase are required for conversion of dodecane to lauric acid in Acinetobacter calcoaceticus ADP1." Geissdoerfer W., Frosch C.S., Haspel G., Ehrt S., Hillen W. Microbiology 141:1425-1432(1995) [PubMed: 7670642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ADP1.
[3]	Kok R.G., Bart A., Hellingwerf K.J. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-392.
[4]	"The genes rubA and rubB for alkane degradation in Acinetobacter sp. strain ADP1 are in an operon with estB, encoding an esterase, and oxyR." Geissdorfer W., Kok R.G., Ratajczak A., Hellingwerf K.J., Hillen W. J. Bacteriol. 181:4292-4298(1999) [PubMed: 10400587] [Abstract] Cited for: FUNCTION IN ALKANE DEGRADATION, INDUCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46863 Genomic DNA. Translation: CAA86926.1. CR543861 Genomic DNA. Translation: CAG67953.1. X88895 Genomic DNA. Translation: CAA61350.1.
RefSeq	YP_045775.1. NC_005966.1.
3D structure databases
ProteinModelPortal	P42454.
ModBase	Search...
Protein-protein interaction databases
STRING	P42454.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2880553.
GenomeReviews	Gene locus ACIAD1065 in contig CR543861_GR.
KEGG	aci:ACIAD1065.
NMPDR	fig|62977.3.peg.1214.
PATRIC	20739982. VBIAciSp98416_0955.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0446.
HOGENOM	HBG542563.
OMA	LAMDMAS.
PhylomeDB	P42454.
ProtClustDB	CLSK707186.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD1065-MONOMER.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
KO	K05297.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
ProtoNet	Search...

Entry information

Entry name

RURE_ACIAD

Accession

Primary (citable) accession number: P42454
Secondary accession number(s): Q6FDA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	August 31, 2004
Last modified:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program