[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7670642 [NCBI, ExPASy, EBI, Israel, Japan] Geissdoerfer W., Frosch C.S., Haspel G., Ehrt S., Hillen W.; "Two genes encoding proteins with similarities to rubredoxin and rubredoxin reductase are required for conversion of dodecane to lauric acid in Acinetobacter calcoaceticus ADP1."; Microbiology 141:1425-1432(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."; Nucleic Acids Res. 32:5766-5779(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-392. Kok R.G., Bart A., Hellingwerf K.J.; Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.

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.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z46863; CAA86926.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR543861; CAG67953.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X88895; CAA61350.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_045775.1; -.

3D structure databases

ModBase

P42454.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1065-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0015044;	Molecular function: rubredoxin-NAD+ reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

ProtoNet

P42454.

Genome annotation databases

GeneID

2880553; -.

GenomeReviews

CR543861_GR; ACIAD1065.

KEGG

aci:ACIAD1065; -.

NMPDR

fig|62977.3.peg.1214; -.

Phylogenomic databases

HOGENOM

P42454; -.

Genome annotation databases

CMR

P42454; ACIAD1065.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 393`	`393`	`Rubredoxin-NAD(+) reductase.`	`PRO_0000167649`
`NP_BIND`	`3 35`	`33`	`FAD (Potential).`
`NP_BIND`	`150 178`	`29`	`NAD (Potential).`
`NP_BIND`	`272 282`	`11`	`FAD.`
`CONFLICT`	`75 77`		`LSE -> SSD (in Ref. 1).`
`CONFLICT`	`199 204`		`NLEESG -> IWRKR (in Ref. 1).`

Sequence information

Length: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 42464 Da [This is the MW of the unprocessed precursor]

CRC64: 2A126C8FC3AB1DA2 [This is a checksum on the sequence]

        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

P42454 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools