[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3622516 [NCBI, ExPASy, EBI, Israel, Japan] Brandsch R., Hinkkanen A.E., Mauch L., Nagursky H., Decker K.; "6-hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase."; Eur. J. Biochem. 167:315-320(1987).
[2]	SEQUENCE REVISION. Brandsch R.; Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
[3]	FLAVIN BINDING AT HIS-71, AND MUTAGENESIS OF HIS-71. DOI=10.1016/0014-5793(89)81792-2; PubMed=2680607 [NCBI, ExPASy, EBI, Israel, Japan] Mauch L., Bichler V., Brandsch R.; "Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity."; FEBS Lett. 257:86-88(1989).
[4]	MUTAGENESIS OF ARG-67 AND SER-68. PubMed=2115879 [NCBI, ExPASy, EBI, Israel, Japan] Mauch L., Bichler V., Brandsch R.; "Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase."; J. Biol. Chem. 265:12761-12762(1990).

Comments

CATALYTIC ACTIVITY: (R)-6-hydroxynicotine + H₂O + O₂ = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H₂O₂.
COFACTOR: FAD.
PATHWAY: Alkaloid degradation; nicotine degradation .
SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.

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

X05999; CAA29416.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00087; DEIQHN.

3D structure databases

SMR

P08159; 4-456.

ModBase

P08159.

Ontologies

GO:0018530;	Molecular function: (R)-6-hydroxynicotine oxidase 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

IPR012951; BBE.
IPR006094; Oxid_FAD_bind_N.
IPR006093; Oxy_OxRdtase_FAD_BS.
Graphical view of domain structure.

Pfam

PF08031; BBE; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PS00862; OX2_COVAL_FAD; 1.
PROSITE graphical view of domain structure (profiles).

Other

P08159; -.

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

Keywords

FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 458`	`458`	`6-hydroxy-D-nicotine oxidase.`	`PRO_0000128157`
`DOMAIN`	`33 204`	`172`	`FAD-binding PCMH-type.`
`MOD_RES`	`71 71`		`Tele-8alpha-FAD histidine.`
`MUTAGEN`	`67 67`		`R->A: No FAD incorporation.`
`MUTAGEN`	`67 67`		`R->K: No effect on FAD incorporation, but reduces activity.`
`MUTAGEN`	`68 68`		`S->A: No effect on FAD incorporation or on activity.`
`MUTAGEN`	`71 71`		`H->C,Y,S: No FAD incorporation, abolishes or diminishes significantly the activity.`

Sequence information

Length: 458 AA [This is the length of the unprocessed precursor]

Molecular weight: 48786 Da [This is the MW of the unprocessed precursor]

CRC64: 6783E444D66DC841 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSKLATPLS IQGEVIYPDD SGFDAIANIW DGRHLQRPSL IARCLSAGDV AKSVRYACDN 

        70         80         90        100        110        120 
GLEISVRSGG HNPNGYATND GGIVLDLRLM NSIHIDTAGS RARIGGGVIS GDLVKEAAKF 

       130        140        150        160        170        180 
GLAAVTGMHP KVGFCGLALN GGVGFLTPKY GLASDNILGA TLVTATGDVI YCSDDERPEL 

       190        200        210        220        230        240 
FWAVRGAGPN FGVVTEVEVQ LYELPRKMLA GFITWAPSVS ELAGLLTSLL DALNEMADHI 

       250        260        270        280        290        300 
YPSVFVGVDE NRAPSVTVCV GHLGGLDIAE RDIARLRGLG RTVSDSIAVR SYDEVVALNA 

       310        320        330        340        350        360 
EVGSFEDGMS NLWIDREIAM PNARFAEAIA GNLDKFVSEP ASGGSVKLEI EGMPFGNPKR 

       370        380        390        400        410        420 
TPARHRDAMG VLALAEWSGA APGSEKYPEL ARELDAALLR AGVTTSGFGL LNNNSEVTAE 

       430        440        450 
MVAEVYKPEV YCRLAAVKRE YDPENRFRHN YNIDPEGS

P08159 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