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Protein

2,6-dihydropseudooxynicotine hydrolase

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

Functioni

L-nicotine is used as a growth substrate. Plays a role in nicotine catabolism by cleaving a C-C bond in 2,6-dihydroxypseudooxynicotine.2 Publications

Catalytic activityi

1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O = 2,6-dihydroxypyridine + 4-methylaminobutanoate.2 Publications

Kineticsi

  1. KM=6 µM for 2,6-dihydropseudooxynicotine1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Pathwayi: nicotine degradation

    This protein is involved in step 2 of the subpathway that synthesizes 2,6-dihydroxypyridine and 4-(methylamino)butanoate from 6-hydroxypseudooxynicotine.3 Publications
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. 2,6-dihydropseudooxynicotine hydrolase
    This subpathway is part of the pathway nicotine degradation, which is itself part of Alkaloid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2,6-dihydroxypyridine and 4-(methylamino)butanoate from 6-hydroxypseudooxynicotine, the pathway nicotine degradation and in Alkaloid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei148 – 14811 PublicationSequence analysis
    Active sitei217 – 21711 Publication
    Active sitei300 – 30011 Publication
    Active sitei329 – 32911 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Alkaloid metabolism

    Enzyme and pathway databases

    BRENDAi3.7.1.19. 449.
    SABIO-RKQ93NG6.
    UniPathwayiUPA00106; UER00490.

    Protein family/group databases

    ESTHERiartni-Q93NG6. Duf_1100.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,6-dihydropseudooxynicotine hydrolase (EC:3.7.1.19)
    Encoded oniPlasmid pAO1Imported
    OrganismiArthrobacter nicotinovorans
    Taxonomic identifieri29320 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181R → A: Total loss of activity. 1 Publication
    Mutagenesisi22 – 221D → A: 91% loss of activity. 1 Publication
    Mutagenesisi148 – 1481E → A: 98% loss of activity. 1 Publication
    Mutagenesisi149 – 1491S → A: 84% loss of activity. 1 Publication
    Mutagenesisi153 – 1531E → A: 32% loss of activity. 1 Publication
    Mutagenesisi216 – 2161R → A: 92% loss of activity. 1 Publication
    Mutagenesisi217 – 2171S → A: Total loss of activity. 1 Publication
    Mutagenesisi300 – 3001D → A: 94% loss of activity. 1 Publication
    Mutagenesisi329 – 3291H → A: 92% loss of activity. 1 Publication
    Mutagenesisi330 – 3301C → A: 5% loss of activity. 1 Publication
    Mutagenesisi332 – 3321H → A: 58% loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3673672,6-dihydropseudooxynicotine hydrolasePRO_0000283735Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 135Combined sources
    Helixi16 – 227Combined sources
    Helixi26 – 338Combined sources
    Helixi41 – 6121Combined sources
    Helixi65 – 8319Combined sources
    Helixi90 – 10516Combined sources
    Helixi106 – 1083Combined sources
    Beta strandi109 – 1113Combined sources
    Beta strandi113 – 1208Combined sources
    Beta strandi123 – 1308Combined sources
    Beta strandi133 – 1353Combined sources
    Beta strandi138 – 1447Combined sources
    Turni151 – 1533Combined sources
    Helixi155 – 1639Combined sources
    Beta strandi167 – 1715Combined sources
    Helixi177 – 1793Combined sources
    Turni180 – 1823Combined sources
    Helixi189 – 20214Combined sources
    Beta strandi206 – 21611Combined sources
    Helixi218 – 22912Combined sources
    Beta strandi235 – 2406Combined sources
    Helixi248 – 2503Combined sources
    Helixi253 – 26210Combined sources
    Helixi268 – 27811Combined sources
    Turni282 – 2843Combined sources
    Helixi285 – 2873Combined sources
    Beta strandi292 – 2976Combined sources
    Beta strandi300 – 3023Combined sources
    Helixi305 – 3139Combined sources
    Helixi316 – 3183Combined sources
    Beta strandi319 – 3246Combined sources
    Helixi329 – 3346Combined sources
    Helixi337 – 35014Combined sources
    Beta strandi360 – 3623Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JBWX-ray2.10A/B/C/D1-365[»]
    ProteinModelPortaliQ93NG6.
    SMRiQ93NG6. Positions 15-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93NG6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UPF0255 family.Sequence analysis

    Phylogenomic databases

    KOiK19188.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR010520. UPF0255.
    [Graphical view]
    PfamiPF06500. DUF1100. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q93NG6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVTSQVKPE DEMLNWGRLI LDGVSYSDMV GARDRPKEIT WFDYWMSLAN
    60 70 80 90 100
    EYEQEAERKV ALGHDLSAGE LLMSAALCAQ YAQFLWFDER RQKGQARKVE
    110 120 130 140 150
    LYQKAAPLLS PPAERHELVV DGIPMPVYVR IPEGPGPHPA VIMLGGLEST
    160 170 180 190 200
    KEESFQMENL VLDRGMATAT FDGPGQGEMF EYKRIAGDYE KYTSAVVDLL
    210 220 230 240 250
    TKLEAIRNDA IGVLGRSLGG NYALKSAACE PRLAACISWG GFSDLDYWDL
    260 270 280 290 300
    ETPLTKESWK YVSKVDTLEE ARLHVHAALE TRDVLSQIAC PTYILHGVHD
    310 320 330 340 350
    EVPLSFVDTV LELVPAEHLN LVVEKDGDHC CHNLGIRPRL EMADWLYDVL
    360
    VAGKKVAPTM KGWPLNG
    Length:367
    Mass (Da):40,995
    Last modified:December 1, 2001 - v1
    Checksum:i1A5D31A7DFC4C8E3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF373840 Genomic DNA. Translation: AAK64252.1.
    AJ507836 Genomic DNA. Translation: CAD47941.1.
    RefSeqiWP_016359452.1. NC_021229.1.
    YP_007988767.1. NC_021229.1.

    Genome annotation databases

    GeneIDi15879627.
    KEGGiag:CAD47941.
    pg:15879627.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF373840 Genomic DNA. Translation: AAK64252.1.
    AJ507836 Genomic DNA. Translation: CAD47941.1.
    RefSeqiWP_016359452.1. NC_021229.1.
    YP_007988767.1. NC_021229.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JBWX-ray2.10A/B/C/D1-365[»]
    ProteinModelPortaliQ93NG6.
    SMRiQ93NG6. Positions 15-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERiartni-Q93NG6. Duf_1100.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi15879627.
    KEGGiag:CAD47941.
    pg:15879627.

    Phylogenomic databases

    KOiK19188.

    Enzyme and pathway databases

    UniPathwayiUPA00106; UER00490.
    BRENDAi3.7.1.19. 449.
    SABIO-RKQ93NG6.

    Miscellaneous databases

    EvolutionaryTraceiQ93NG6.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR010520. UPF0255.
    [Graphical view]
    PfamiPF06500. DUF1100. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    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].
    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].
    3. "The bacterial oxidation of nicotine. VI. The metabolism of 2,6-dihydroxypseudooxynicotine."
      Gherna R.L., Richardson S.H., Rittenberg S.C.
      J. Biol. Chem. 240:3669-3674(1965) [PubMed] [Europe PMC] [Abstract]
      Cited for: PATHWAY.
    4. "An alpha/beta-fold C--C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans."
      Sachelaru P., Schiltz E., Igloi G.L., Brandsch R.
      J. Bacteriol. 187:8516-8519(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
    5. "Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation."
      Schleberger C., Sachelaru P., Brandsch R., Schulz G.E.
      J. Mol. Biol. 367:409-418(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ARG-18; ASP-22; GLU-148; SER-149; GLU-153; ARG-216; SER-217; ASP-300; HIS-329; CYS-330 AND HIS-332.

    Entry informationi

    Entry nameiDHPON_ARTNI
    AccessioniPrimary (citable) accession number: Q93NG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: December 1, 2001
    Last modified: July 6, 2016
    This is version 64 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
    3. SIMILARITY comments
      Index of protein domains and families
    4. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    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.