Q93NG3 (Q93NG3_ARTNI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
2,6-dihydroxypyridine hydroxylase EMBL CAD47937.1

Submitted name:
Dhph EMBL AAK64255.1

Gene names

Name:

dhph EMBL CAD47937.1

Encoded on

Plasmid pA01 Ref.7 Ref.8 EMBL AAK64255.1
Plasmid pAO1 Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 EMBL CAD47937.1

Organism

Arthrobacter nicotinovorans EMBL AAK64255.1

Taxonomic identifier

29320 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	FAD PDB 2VOU Flavoprotein PDB 2VOU Nucleotide-binding PDB 2VOU
Technical term	3D-structure PDB 2VOU Plasmid EMBL AAK64255.1
Gene Ontology (GO)
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	14 – 16	3	FAD PDB 2VOU
	Nucleotide binding	35 – 36	2	FAD PDB 2VOU
	Nucleotide binding	316 – 320	5	FAD PDB 2VOU
Sites
	Binding site	49	1	FAD; via amide nitrogen and carbonyl oxygen PDB 2VOU
	Binding site	120	1	FAD; via amide nitrogen and carbonyl oxygen PDB 2VOU
	Binding site	306	1	FAD PDB 2VOU

Sequences

	Sequence		Length	Mass (Da)
	Q93NG3 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: D257CDC11D516CBE	FASTA	397	43,400
	10 20 30 40 50 60 MSPTTDRIAV VGGSISGLTA ALMLRDAGVD VDVYERSPQP LSGFGTGIVV QPELVHYLLE 70 80 90 100 110 120 QGVELDSISV PSSSMEYVDA LTGERVGSVP ADWRFTSYDS IYGGLYELFG PERYHTSKCL 130 140 150 160 170 180 VGLSQDSETV QMRFSDGTKA EANWVIGADG GASVVRKRLL GIEPTYAGYV TWRGVLQPGE 190 200 210 220 230 240 VADDVWNYFN DKFTYGLLDD GHLIAYPIPG RENAESPRLN FQWYWNVAEG PDLDELMTDV 250 260 270 280 290 300 RGIRLPTSVH NNSLNPHNLR QFHSKGESLF KPFRDLVLNA SSPFVTVVAD ATVDRMVHGR 310 320 330 340 350 360 VLLIGDAAVT PRPHAAAGGA KACDDARTLA EVFTKNHDLR GSLQSWETRQ LQQGHAYLNK 370 380 390 VKKMASRLQH GGSFEPGNPA FAFGLPKVDE PSVVTNS

References

[1]	"Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial plasmid: characterization of MoeA as a filament-forming protein with adenosinetriphosphatase activity." Menendez C., Otto A., Igloi G., Nick P., Brandsch R., Schubach B., Boettcher B., Brandsch R. Eur. J. Biochem. 250:524-531(1997) [PubMed: 9428706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans." Grether-Beck S., Igloi G.L., Pust S., Schilz E., Decker K., Brandsch R. Mol. Microbiol. 13:929-936(1994) [PubMed: 7815950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"IS1473, a putative insertion sequence identified in the plasmid pAO1 from Arthrobacter nicotinovorans: isolation, characterization, and distribution among Arthrobacter species." Menendez C., Igloi G.L., Brandsch R. Plasmid 37:35-41(1997) [PubMed: 9073580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[4]	"A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein." Menendez C., Igloi G., Henninger H., Brandsch R. Arch. Microbiol. 164:142-151(1995) [PubMed: 8588735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[5]	"Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter nicotinovorans and identification of a pAO1-dependent nicotine uptake system." Igloi G.L., Brandsch R. J. Bacteriol. 185:1976-1986(2003) [PubMed: 12618462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[6]	"Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans." Schenk S., Hoelz A., Krauss B., Decker K. J. Mol. Biol. 284:1323-1339(1998) [PubMed: 9878353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[7]	"Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway." Treiber N., Schulz G.E. J. Mol. Biol. 379:94-104(2008) [PubMed: 18440023] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FAD.
[8]	"Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase." Baitsch D., Sandu C., Brandsch R., Igloi G.L. J. Bacteriol. 183:5262-5267(2001) [PubMed: 11514508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF373840 Genomic DNA. Translation: AAK64255.1.
AJ507836 Genomic DNA. Translation: CAD47937.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VOU	X-ray	2.60	A/B/C	1-397	[»]

ProteinModelPortal

Q93NG3.

SMR

Q93NG3. Positions 2-394.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR002938. mOase_FAD-bd.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR003042. Rng_hydrolase-like.
[Graphical view]

Pfam

PF01494. FAD_binding_3. 1 hit.
PF00070. Pyr_redox. 1 hit.
[Graphical view]

PRINTS

PR00420. RNGMNOXGNASE.

ProtoNet

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Entry information

Entry name

Q93NG3_ARTNI

Accession

Primary (citable) accession number: Q93NG3

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)