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Protein

Nitroalkane oxidase

Gene
N/A
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative denitrification of neutral nitroalkanes, including 3-nitro-2-pentanol, 1-nitropropane, 2-nitropropane, nitroethane and nitrocyclohexane, and may thereby protect the organism against toxic compounds. Has no detectable acyl-CoA dehydrogenase activity.3 Publications

Catalytic activityi

A nitroalkane + H2O + O2 = an aldehyde or ketone + nitrite + H2O2.5 Publications

Cofactori

FAD6 Publications

Enzyme regulationi

Strongly inhibited by mercury chloride and KCN.1 Publication

Kineticsi

  1. KM=1.54 mM for 1-nitropropane1 Publication
  2. KM=7.4 mM for 2-nitropropane1 Publication
  3. KM=1.0 mM for nitroethane1 Publication
  4. KM=3.1 mM for 3-nitro-2-pentanol1 Publication
  5. KM=0.9 mM for nitrocyclohexane1 Publication
  6. KM=1.33 µM for FAD1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei304 – 3041FAD3 Publications
    Active sitei402 – 4021Proton acceptor3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi131 – 1344FAD3 Publications
    Nucleotide bindingi139 – 1413FAD3 Publications
    Nucleotide bindingi169 – 1713FAD3 Publications
    Nucleotide bindingi313 – 3142FAD3 Publications
    Nucleotide bindingi375 – 3795FAD3 Publications
    Nucleotide bindingi400 – 4045FAD3 Publications

    GO - Molecular functioni

    • FAD binding Source: UniProtKB
    • nitroalkane oxidase activity Source: UniProtKB
    • nitroethane oxidase activity Source: UniProtKB-EC
    • oxidoreductase activity, acting on the CH-CH group of donors Source: InterPro

    GO - Biological processi

    • nitrogen compound metabolic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12547.
    BRENDAi1.7.3.1. 2351.
    SABIO-RKQ8X1D8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitroalkane oxidase (EC:1.7.3.1)
    Short name:
    NAO
    OrganismiFusarium oxysporum (Fusarium vascular wilt)
    Taxonomic identifieri5507 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi276 – 2761S → A: Decreases catalytic activity about tenfold. 1 Publication
    Mutagenesisi402 – 4021D → E: Decreases enzyme activity about twentyfold. 3 Publications
    Mutagenesisi402 – 4021D → N: Almost abolishes enzyme activity towards neutral nitroethane, but retains activity towards anionic nitroethane. 3 Publications
    Mutagenesisi409 – 4091R → K: Reduces catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Nitroalkane oxidasePRO_0000418397Add
    BLAST

    Expressioni

    Inductioni

    Up-regulated by nitroethane.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Protein-protein interaction databases

    STRINGi5507.FOXG_08703P0.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2316Combined sources
    Helixi25 – 273Combined sources
    Helixi28 – 325Combined sources
    Helixi38 – 436Combined sources
    Helixi46 – 549Combined sources
    Turni55 – 584Combined sources
    Helixi59 – 613Combined sources
    Helixi64 – 663Combined sources
    Helixi73 – 8412Combined sources
    Helixi91 – 10616Combined sources
    Helixi110 – 1167Combined sources
    Helixi118 – 1214Combined sources
    Beta strandi129 – 1324Combined sources
    Turni140 – 1434Combined sources
    Beta strandi153 – 1575Combined sources
    Beta strandi160 – 1689Combined sources
    Turni171 – 1777Combined sources
    Beta strandi182 – 1909Combined sources
    Helixi204 – 2074Combined sources
    Beta strandi208 – 2136Combined sources
    Helixi215 – 2195Combined sources
    Helixi223 – 2253Combined sources
    Beta strandi226 – 2305Combined sources
    Beta strandi234 – 2363Combined sources
    Beta strandi244 – 25310Combined sources
    Helixi254 – 2563Combined sources
    Helixi263 – 30139Combined sources
    Beta strandi306 – 3083Combined sources
    Helixi310 – 3123Combined sources
    Helixi314 – 34128Combined sources
    Beta strandi344 – 3463Combined sources
    Helixi348 – 37730Combined sources
    Helixi379 – 3824Combined sources
    Helixi388 – 3958Combined sources
    Turni396 – 4005Combined sources
    Beta strandi401 – 4033Combined sources
    Turni405 – 4084Combined sources
    Helixi409 – 4179Combined sources
    Helixi426 – 4294Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C0UX-ray2.20A/B/C/D1-439[»]
    2C12X-ray2.07A/B/C/D/E/F1-439[»]
    2REHX-ray2.40A/B/C/D1-439[»]
    2ZAFX-ray2.50A/B/C/D1-439[»]
    3D9DX-ray2.10A/B/C/D2-439[»]
    3D9EX-ray2.20A/B/C/D2-439[»]
    3D9FX-ray2.20A/B/C/D2-439[»]
    3D9GX-ray2.15A/B/C/D2-439[»]
    3FCJX-ray2.40A/B/C/D2-439[»]
    ProteinModelPortaliQ8X1D8.
    SMRiQ8X1D8. Positions 2-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8X1D8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiKOG0140. Eukaryota.
    COG1960. LUCA.
    KOiK19823.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8X1D8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVDFKLSPSQ LEARRHAQAF ANTVLTKASA EYSTQKDQLS RFQATRPFYR
    60 70 80 90 100
    EAVRHGLIKA QVPIPLGGTM ESLVHESIIL EELFAVEPAT SITIVATALG
    110 120 130 140 150
    LMPVILCDSP SLQEKFLKPF ISGEGEPLAS LMHSEPNGTA NWLQKGGPGL
    160 170 180 190 200
    QTTARKVGNE WVISGEKLWP SNSGGWDYKG ADLACVVCRV SDDPSKPQDP
    210 220 230 240 250
    NVDPATQIAV LLVTRETIAN NKKDAYQILG EPELAGHITT SGPHTRFTEF
    260 270 280 290 300
    HVPHENLLCT PGLKAQGLVE TAFAMSAALV GAMAIGTARA AFEEALVFAK
    310 320 330 340 350
    SDTRGGSKHI IEHQSVADKL IDCKIRLETS RLLVWKAVTT LEDEALEWKV
    360 370 380 390 400
    KLEMAMQTKI YTTDVAVECV IDAMKAVGMK SYAKDMSFPR LLNEVMCYPL
    410 420 430
    FDGGNIGLRR RQMQRVMALE DYEPWAATYG SSKVDKSRL
    Length:439
    Mass (Da):48,162
    Last modified:March 1, 2002 - v1
    Checksum:i9F156889F2A5901A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF425595 mRNA. Translation: AAL57485.1.

    Genome annotation databases

    KEGGiag:AAL57485.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF425595 mRNA. Translation: AAL57485.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C0UX-ray2.20A/B/C/D1-439[»]
    2C12X-ray2.07A/B/C/D/E/F1-439[»]
    2REHX-ray2.40A/B/C/D1-439[»]
    2ZAFX-ray2.50A/B/C/D1-439[»]
    3D9DX-ray2.10A/B/C/D2-439[»]
    3D9EX-ray2.20A/B/C/D2-439[»]
    3D9FX-ray2.20A/B/C/D2-439[»]
    3D9GX-ray2.15A/B/C/D2-439[»]
    3FCJX-ray2.40A/B/C/D2-439[»]
    ProteinModelPortaliQ8X1D8.
    SMRiQ8X1D8. Positions 2-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5507.FOXG_08703P0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAL57485.

    Phylogenomic databases

    eggNOGiKOG0140. Eukaryota.
    COG1960. LUCA.
    KOiK19823.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12547.
    BRENDAi1.7.3.1. 2351.
    SABIO-RKQ8X1D8.

    Miscellaneous databases

    EvolutionaryTraceiQ8X1D8.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    InterProiIPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily."
      Daubner S.C., Gadda G., Valley M.P., Fitzpatrick P.F.
      Proc. Natl. Acad. Sci. U.S.A. 99:2702-2707(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-402, ACTIVE SITE, COFACTOR.
      Strain: ATCC 695.
    2. "Purification and properties of nitroalkane oxidase from Fusarium oxysporum."
      Kido T., Hashizume K., Soda K.
      J. Bacteriol. 133:53-58(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, ENZYME REGULATION, INDUCTION.
      Strain: ATCC 659 / NBRC 5942 / DR 1004.
    3. "Inactivation of nitroalkane oxidase upon mutation of the active site base and rescue with a deprotonated substrate."
      Valley M.P., Fitzpatrick P.F.
      J. Am. Chem. Soc. 125:8738-8739(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-402.
    4. "Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover."
      Nagpal A., Valley M.P., Fitzpatrick P.F., Orville A.M.
      Biochemistry 45:1138-1150(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE NITROBUTANE AND FAD, FUNCTION, COFACTOR, ACTIVE SITE, SUBUNIT.
    5. "Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase."
      Fitzpatrick P.F., Bozinovski D.M., Heroux A., Shaw P.G., Valley M.P., Orville A.M.
      Biochemistry 46:13800-13808(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT LYS-409 IN COMPLEX WITH FAD, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-409.
    6. "Crystal structures of intermediates in the nitroalkane oxidase reaction."
      Heroux A., Bozinovski D.M., Valley M.P., Fitzpatrick P.F., Orville A.M.
      Biochemistry 48:3407-3416(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS ALA-276 AND ASN-402 IN COMPLEXES WITH THE SUBSTRATE 1-NITROHEXANE AND FAD, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF SER-276 AND ASP-402.
    7. "Differential quantum tunneling contributions in nitroalkane oxidase catalyzed and the uncatalyzed proton transfer reaction."
      Major D.T., Heroux A., Orville A.M., Valley M.P., Fitzpatrick P.F., Gao J.
      Proc. Natl. Acad. Sci. U.S.A. 106:20734-20739(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ASN-402 IN COMPLEX WITH FAD AND THE SUBSTRATE NITROETHANE, COFACTOR.

    Entry informationi

    Entry nameiNAO_FUSOX
    AccessioniPrimary (citable) accession number: Q8X1D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: March 1, 2002
    Last modified: May 11, 2016
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    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.