ID   HDNO_ARTOX              Reviewed;         458 AA.
AC   P08159;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=6-hydroxy-D-nicotine oxidase;
DE            Short=6-HDNO;
DE            EC=1.5.3.6;
OS   Arthrobacter oxidans.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87304263; PubMed=3622516;
RX   DOI=10.1111/j.1432-1033.1987.tb13338.x;
RA   Brandsch R., Hinkkanen A.E., Mauch L., Nagursky H., Decker K.;
RT   "6-hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure
RT   of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine
RT   oxidase.";
RL   Eur. J. Biochem. 167:315-320(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Brandsch R.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FLAVIN BINDING AT HIS-71, AND MUTAGENESIS OF HIS-71.
RX   MEDLINE=90033359; PubMed=2680607; DOI=10.1016/0014-5793(89)81792-2;
RA   Mauch L., Bichler V., Brandsch R.;
RT   "Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-
RT   D-nicotine oxidase. Consequences on flavinylation and enzyme
RT   activity.";
RL   FEBS Lett. 257:86-88(1989).
RN   [4]
RP   MUTAGENESIS OF ARG-67 AND SER-68.
RX   MEDLINE=90330600; PubMed=2115879;
RA   Mauch L., Bichler V., Brandsch R.;
RT   "Lysine can replace arginine 67 in the mediation of covalent
RT   attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase.";
RL   J. Biol. Chem. 265:12761-12762(1990).
CC   -!- CATALYTIC ACTIVITY: (R)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-
CC       hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; X05999; CAA29416.1; -; Genomic_DNA.
DR   PIR; S00087; DEIQHN.
DR   SMR; P08159; 4-456.
DR   GO; GO:0018530; F:(R)-6-hydroxynicotine oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    458       6-hydroxy-D-nicotine oxidase.
FT                                /FTId=PRO_0000128157.
FT   DOMAIN       33    204       FAD-binding PCMH-type.
FT   MOD_RES      71     71       Tele-8alpha-FAD histidine.
FT   MUTAGEN      67     67       R->A: No FAD incorporation.
FT   MUTAGEN      67     67       R->K: No effect on FAD incorporation, but
FT                                reduces activity.
FT   MUTAGEN      68     68       S->A: No effect on FAD incorporation or
FT                                on activity.
FT   MUTAGEN      71     71       H->C,Y,S: No FAD incorporation, abolishes
FT                                or diminishes significantly the activity.
SQ   SEQUENCE   458 AA;  48786 MW;  6783E444D66DC841 CRC64;
     MSSKLATPLS IQGEVIYPDD SGFDAIANIW DGRHLQRPSL IARCLSAGDV AKSVRYACDN
     GLEISVRSGG HNPNGYATND GGIVLDLRLM NSIHIDTAGS RARIGGGVIS GDLVKEAAKF
     GLAAVTGMHP KVGFCGLALN GGVGFLTPKY GLASDNILGA TLVTATGDVI YCSDDERPEL
     FWAVRGAGPN FGVVTEVEVQ LYELPRKMLA GFITWAPSVS ELAGLLTSLL DALNEMADHI
     YPSVFVGVDE NRAPSVTVCV GHLGGLDIAE RDIARLRGLG RTVSDSIAVR SYDEVVALNA
     EVGSFEDGMS NLWIDREIAM PNARFAEAIA GNLDKFVSEP ASGGSVKLEI EGMPFGNPKR
     TPARHRDAMG VLALAEWSGA APGSEKYPEL ARELDAALLR AGVTTSGFGL LNNNSEVTAE
     MVAEVYKPEV YCRLAAVKRE YDPENRFRHN YNIDPEGS
//