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Reviewed, UniProtKB/Swiss-Prot P08159 (HDNO_ARTOX)

Last modified June 16, 2009. Version 60. 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

Names and origin

Protein namesRecommended name:
    6-hydroxy-D-nicotine oxidase
      Short name=6-HDNO
    EC=1.5.3.6
OrganismArthrobacter oxidans
Taxonomic identifier1671 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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.

Sequence similarities

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4584586-hydroxy-D-nicotine oxidase
PRO_0000128157

Regions

Domain33 – 204172FAD-binding PCMH-type

Amino acid modifications

Modified residue711Tele-8alpha-FAD histidine

Experimental info

Mutagenesis671R → A: No FAD incorporation. Ref.4
Mutagenesis671R → K: No effect on FAD incorporation, but reduces activity. Ref.4
Mutagenesis681S → A: No effect on FAD incorporation or on activity. Ref.4
Mutagenesis711H → C, Y or S: No FAD incorporation, abolishes or diminishes significantly the activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08159-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 6783E444D66DC841

FASTA45848,786
        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 

« Hide

References

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

Cross-references

Sequence databases

X05999 Genomic DNA. Translation: CAA29416.1.
PIRDEIQHN. S00087.

3D structure databases

SMRP08159. Positions 4-456.
ModBaseSearch...

Family and domain databases

InterProIPR012951. BBE.
IPR016166. FAD-bd_2.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDNO_ARTOX
AccessionPrimary (citable) accession number: P08159
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 60 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)

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