P08159 (HDNO_ARTOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 6-hydroxy-D-nicotine oxidase Short name=6-HDNO EC=1.5.3.6
Organism	Arthrobacter oxidans
Taxonomic identifier	1671 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Molecular function	(R)-6-hydroxynicotine oxidase activity Inferred from electronic annotation. Source: EC UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 458	458	6-hydroxy-D-nicotine oxidase		PRO_0000128157
Regions
	Domain	33 – 204	172	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	71	1	Pros-8alpha-FAD histidine
Experimental info
	Mutagenesis	67	1	R → A: No FAD incorporation. Ref.4
	Mutagenesis	67	1	R → K: No effect on FAD incorporation, but reduces activity. Ref.4
	Mutagenesis	68	1	S → A: No effect on FAD incorporation or on activity. Ref.4
	Mutagenesis	71	1	H → C, Y or S: No FAD incorporation, abolishes or diminishes significantly the activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P08159 [UniParc]. Last modified May 1, 1991. Version 2. Checksum: 6783E444D66DC841	FASTA	458	48,786
	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

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
EMBL GenBank DDBJ	X05999 Genomic DNA. Translation: CAA29416.1.
PIR	DEIQHN. S00087.
3D structure databases
ProteinModelPortal	P08159.
SMR	P08159. Positions 4-456.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR012951. BBE. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR006094. Oxid_FAD_bind_N. IPR006093. Oxy_OxRdtase_FAD_BS. [Graphical view]
Gene3D	G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
Pfam	PF08031. BBE. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
SUPFAM	SSF56176. FAD-binding_2. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. PS00862. OX2_COVAL_FAD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDNO_ARTOX

Accession

Primary (citable) accession number: P08159

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 1, 1991
Last modified:	October 19, 2011
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program