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Reviewed, UniProtKB/Swiss-Prot P42454 (RURE_ACIAD)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Rubredoxin-NAD(+) reductase
    EC=1.18.1.1
Gene names
Name: rubB
Ordered Locus Names: ACIAD1065
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

N-alkanes are oxidized by a 3-component enzyme system, alkane hydroxylase, rubredoxin and rubredoxin reductase.

Catalytic activity

2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH.

Cofactor

FAD.

Pathway

Hydrocarbon metabolism; alkane degradation.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

rubredoxin-NAD+ reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Rubredoxin-NAD(+) reductase
PRO_0000167649

Regions

Nucleotide binding3 – 3533FAD Potential
Nucleotide binding150 – 17829NAD Potential
Nucleotide binding272 – 28211FAD

Experimental info

Sequence conflict75 – 773LSE → SSD Ref.1
Sequence conflict199 – 2046NLEESG → IWRKR Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P42454-1 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 2A126C8FC3AB1DA2

FASTA39342,464
        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

« Hide

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References

« Hide '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].
[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.

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Cross-references

Sequence databases

Z46863 Genomic DNA. Translation: CAA86926.1.
CR543861 Genomic DNA. Translation: CAG67953.1.
X88895 Genomic DNA. Translation: CAA61350.1.
RefSeqYP_045775.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2880553.
GenomeReviewsGene locus ACIAD1065 in contig CR543861_GR.
KEGGaci:ACIAD1065.
NMPDRfig|62977.3.peg.1214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP42454.
OMAP42454. MICADDA.

Enzyme and pathway databases

BioCycASP62977:ACIAD1065-MON.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

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Entry information

Entry nameRURE_ACIAD
AccessionPrimary (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: June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents