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Protein

2,6-dihydroxypyridine 3-monooxygenase

Gene

dhpH

Organism
Arthrobacter nicotinovorans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 2,6-dihydroxypyridine into 2,3,6-trihydroxypyridine in the nicotine degradation pathway.1 Publication

Catalytic activityi

2,6-dihydroxypyridine + NADH + O2 = 2,3,6-trihydroxypyridine + NAD+ + H2O.1 Publication

Cofactori

FAD1 Publication

Kineticsi

  1. KM=0.0000083 M for 2,6-dihydroxypyridine1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 20 degrees Celsius.1 Publication

    Pathwayi: nicotine degradation

    This protein is involved in the pathway nicotine degradation, which is part of Alkaloid degradation.1 Publication
    View all proteins of this organism that are known to be involved in the pathway nicotine degradation and in Alkaloid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei120 – 1201FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei306 – 3061FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 163FAD1 Publication
    Nucleotide bindingi35 – 362FAD1 Publication
    Nucleotide bindingi316 – 3205FAD1 Publication

    GO - Molecular functioni

    • 2,6-dihydroxypyridine 3-monooxygenase activity Source: UniProtKB
    • flavin adenine dinucleotide binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    • nicotine catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-1001.
    BRENDAi1.14.13.10. 449.
    SABIO-RKQ93NG3.
    UniPathwayiUPA00106.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,6-dihydroxypyridine 3-monooxygenase (EC:1.14.13.10)
    Short name:
    2,6-DHPH
    Gene namesi
    Name:dhpH
    Encoded oniPlasmid pAO12 Publications
    OrganismiArthrobacter nicotinovorans
    Taxonomic identifieri29320 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi323 – 3231C → S: Does not cause structural disturbance. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3973972,6-dihydroxypyridine 3-monooxygenasePRO_0000430255Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116Combined sources
    Helixi15 – 2612Combined sources
    Beta strandi30 – 345Combined sources
    Beta strandi36 – 405Combined sources
    Beta strandi47 – 493Combined sources
    Helixi52 – 609Combined sources
    Helixi65 – 673Combined sources
    Beta strandi74 – 796Combined sources
    Turni80 – 823Combined sources
    Beta strandi85 – 906Combined sources
    Beta strandi95 – 973Combined sources
    Helixi98 – 10912Combined sources
    Beta strandi120 – 1256Combined sources
    Beta strandi130 – 1345Combined sources
    Beta strandi139 – 1479Combined sources
    Helixi154 – 1607Combined sources
    Beta strandi165 – 17612Combined sources
    Helixi183 – 1897Combined sources
    Beta strandi192 – 1987Combined sources
    Beta strandi201 – 2088Combined sources
    Beta strandi218 – 2269Combined sources
    Helixi231 – 2366Combined sources
    Beta strandi246 – 2494Combined sources
    Helixi251 – 2533Combined sources
    Helixi256 – 26611Combined sources
    Helixi271 – 2799Combined sources
    Beta strandi284 – 2918Combined sources
    Beta strandi296 – 2983Combined sources
    Beta strandi301 – 3033Combined sources
    Helixi305 – 3073Combined sources
    Helixi313 – 3153Combined sources
    Helixi318 – 33518Combined sources
    Helixi339 – 36830Combined sources
    Turni369 – 3713Combined sources
    Helixi379 – 3813Combined sources
    Beta strandi382 – 3843Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VOUX-ray2.60A/B/C1-397[»]
    ProteinModelPortaliQ93NG3.
    SMRiQ93NG3. Positions 2-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93NG3.

    Family & Domainsi

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q93NG3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSPTTDRIAV VGGSISGLTA ALMLRDAGVD VDVYERSPQP LSGFGTGIVV
    60 70 80 90 100
    QPELVHYLLE QGVELDSISV PSSSMEYVDA LTGERVGSVP ADWRFTSYDS
    110 120 130 140 150
    IYGGLYELFG PERYHTSKCL VGLSQDSETV QMRFSDGTKA EANWVIGADG
    160 170 180 190 200
    GASVVRKRLL GIEPTYAGYV TWRGVLQPGE VADDVWNYFN DKFTYGLLDD
    210 220 230 240 250
    GHLIAYPIPG RENAESPRLN FQWYWNVAEG PDLDELMTDV RGIRLPTSVH
    260 270 280 290 300
    NNSLNPHNLR QFHSKGESLF KPFRDLVLNA SSPFVTVVAD ATVDRMVHGR
    310 320 330 340 350
    VLLIGDAAVT PRPHAAAGGA KACDDARTLA EVFTKNHDLR GSLQSWETRQ
    360 370 380 390
    LQQGHAYLNK VKKMASRLQH GGSFEPGNPA FAFGLPKVDE PSVVTNS
    Length:397
    Mass (Da):43,400
    Last modified:December 1, 2001 - v1
    Checksum:iD257CDC11D516CBE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF373840 Genomic DNA. Translation: AAK64255.1.
    AJ507836 Genomic DNA. Translation: CAD47937.1.
    RefSeqiWP_016359448.1. NC_021229.1.
    YP_007988763.1. NC_021229.1.

    Genome annotation databases

    GeneIDi15879626.
    KEGGipg:15879626.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF373840 Genomic DNA. Translation: AAK64255.1.
    AJ507836 Genomic DNA. Translation: CAD47937.1.
    RefSeqiWP_016359448.1. NC_021229.1.
    YP_007988763.1. NC_021229.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VOUX-ray2.60A/B/C1-397[»]
    ProteinModelPortaliQ93NG3.
    SMRiQ93NG3. Positions 2-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi15879626.
    KEGGipg:15879626.

    Enzyme and pathway databases

    UniPathwayiUPA00106.
    BioCyciMetaCyc:MONOMER-1001.
    BRENDAi1.14.13.10. 449.
    SABIO-RKQ93NG3.

    Miscellaneous databases

    EvolutionaryTraceiQ93NG3.

    Family and domain databases

    Gene3Di3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    1. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
      Strain: ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511.
      Plasmid: pAO1
    2. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511.
      Plasmid: pAO1
    3. "Finding Sequences for over 270 Orphan Enzymes."
      Shearer A.G., Altman T., Rhee C.D.
      PLoS ONE 9:E97250-E97250(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FAD, MUTAGENESIS OF CYS-323.

    Entry informationi

    Entry nameiDHPH_ARTNI
    AccessioniPrimary (citable) accession number: Q93NG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: December 1, 2001
    Last modified: May 11, 2016
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.