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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)DescriptionActionsGraphical viewLength
    Binding sitei49FAD; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei120FAD; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei306FAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi14 – 16FAD1 Publication3
    Nucleotide bindingi35 – 36FAD1 Publication2
    Nucleotide bindingi316 – 320FAD1 Publication5

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi323C → S: Does not cause structural disturbance. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004302551 – 3972,6-dihydroxypyridine 3-monooxygenaseAdd BLAST397

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Structurei

    Secondary structure

    1397
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Helixi15 – 26Combined sources12
    Beta strandi30 – 34Combined sources5
    Beta strandi36 – 40Combined sources5
    Beta strandi47 – 49Combined sources3
    Helixi52 – 60Combined sources9
    Helixi65 – 67Combined sources3
    Beta strandi74 – 79Combined sources6
    Turni80 – 82Combined sources3
    Beta strandi85 – 90Combined sources6
    Beta strandi95 – 97Combined sources3
    Helixi98 – 109Combined sources12
    Beta strandi120 – 125Combined sources6
    Beta strandi130 – 134Combined sources5
    Beta strandi139 – 147Combined sources9
    Helixi154 – 160Combined sources7
    Beta strandi165 – 176Combined sources12
    Helixi183 – 189Combined sources7
    Beta strandi192 – 198Combined sources7
    Beta strandi201 – 208Combined sources8
    Beta strandi218 – 226Combined sources9
    Helixi231 – 236Combined sources6
    Beta strandi246 – 249Combined sources4
    Helixi251 – 253Combined sources3
    Helixi256 – 266Combined sources11
    Helixi271 – 279Combined sources9
    Beta strandi284 – 291Combined sources8
    Beta strandi296 – 298Combined sources3
    Beta strandi301 – 303Combined sources3
    Helixi305 – 307Combined sources3
    Helixi313 – 315Combined sources3
    Helixi318 – 335Combined sources18
    Helixi339 – 368Combined sources30
    Turni369 – 371Combined sources3
    Helixi379 – 381Combined sources3
    Beta strandi382 – 384Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ93NG3.

    Family & Domainsi

    Phylogenomic databases

    KOiK19189.

    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.
    KEGGiag:AAK64255.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2VOUX-ray2.60A/B/C1-397[»]
    ProteinModelPortaliQ93NG3.
    SMRiQ93NG3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi15879626.
    KEGGiag:AAK64255.

    Phylogenomic databases

    KOiK19189.

    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...

    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: November 30, 2016
    This is version 86 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.