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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)DescriptionActionsGraphical viewLength
    Binding sitei304FAD3 Publications1
    Active sitei402Proton acceptor3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi131 – 134FAD3 Publications4
    Nucleotide bindingi139 – 141FAD3 Publications3
    Nucleotide bindingi169 – 171FAD3 Publications3
    Nucleotide bindingi313 – 314FAD3 Publications2
    Nucleotide bindingi375 – 379FAD3 Publications5
    Nucleotide bindingi400 – 404FAD3 Publications5

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi276S → A: Decreases catalytic activity about tenfold. 1 Publication1
    Mutagenesisi402D → E: Decreases enzyme activity about twentyfold. 3 Publications1
    Mutagenesisi402D → N: Almost abolishes enzyme activity towards neutral nitroethane, but retains activity towards anionic nitroethane. 3 Publications1
    Mutagenesisi409R → K: Reduces catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004183971 – 439Nitroalkane oxidaseAdd BLAST439

    Expressioni

    Inductioni

    Up-regulated by nitroethane.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Protein-protein interaction databases

    STRINGi5507.FOXG_08703P0.

    Structurei

    Secondary structure

    1439
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi8 – 23Combined sources16
    Helixi25 – 27Combined sources3
    Helixi28 – 32Combined sources5
    Helixi38 – 43Combined sources6
    Helixi46 – 54Combined sources9
    Turni55 – 58Combined sources4
    Helixi59 – 61Combined sources3
    Helixi64 – 66Combined sources3
    Helixi73 – 84Combined sources12
    Helixi91 – 106Combined sources16
    Helixi110 – 116Combined sources7
    Helixi118 – 121Combined sources4
    Beta strandi129 – 132Combined sources4
    Turni140 – 143Combined sources4
    Beta strandi153 – 157Combined sources5
    Beta strandi160 – 168Combined sources9
    Turni171 – 177Combined sources7
    Beta strandi182 – 190Combined sources9
    Helixi204 – 207Combined sources4
    Beta strandi208 – 213Combined sources6
    Helixi215 – 219Combined sources5
    Helixi223 – 225Combined sources3
    Beta strandi226 – 230Combined sources5
    Beta strandi234 – 236Combined sources3
    Beta strandi244 – 253Combined sources10
    Helixi254 – 256Combined sources3
    Helixi263 – 301Combined sources39
    Beta strandi306 – 308Combined sources3
    Helixi310 – 312Combined sources3
    Helixi314 – 341Combined sources28
    Beta strandi344 – 346Combined sources3
    Helixi348 – 377Combined sources30
    Helixi379 – 382Combined sources4
    Helixi388 – 395Combined sources8
    Turni396 – 400Combined sources5
    Beta strandi401 – 403Combined sources3
    Turni405 – 408Combined sources4
    Helixi409 – 417Combined sources9
    Helixi426 – 429Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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
    PDB 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.
    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...

    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: November 2, 2016
    This is version 86 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.