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Protein

L-asparagine oxygenase

Gene

asnO

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the 3-hydroxylation of L-asparagine to (2S,3S)-3-hydroxyasparagine. The 3-hydroxylated asparagine produced is incorporated at position 9 during the biosynthesis of the non-ribosomally synthesized calcium-dependent antibiotic (CDA), a 11-residue acidic lipopeptide lactone. Is able to hydroxylate only free L-asparagine, since it hydroxylates neither a CDA analog with unmodified Asn at position 9 nor a peptidyl-carrier-protein (PCP)-bound asparagine. Is not active toward D-asparagine.2 Publications

Catalytic activityi

L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2.1 Publication

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Kineticsi

  1. KM=479 µM for L-asparagine1 Publication

    Pathwayi: calcium-dependent antibiotic biosynthesis

    This protein is involved in the pathway calcium-dependent antibiotic biosynthesis, which is part of Antibiotic biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway calcium-dependent antibiotic biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei125 – 1251L-asparagine1 Publication
    Binding sitei146 – 1461L-asparagine1 Publication
    Metal bindingi155 – 1551Iron1 Publication
    Metal bindingi157 – 1571Iron1 Publication
    Binding sitei157 – 1571L-asparagine1 Publication
    Binding sitei158 – 1581L-asparagine1 Publication
    Metal bindingi287 – 2871Iron1 Publication
    Binding sitei301 – 30112-oxoglutarate1 Publication
    Binding sitei305 – 3051L-asparagine1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.14.11.39. 5998.
    1.14.11.B11. 5998.
    UniPathwayiUPA00979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-asparagine oxygenase (EC:1.14.11.39)
    Alternative name(s):
    L-asparagine 3-hydroxylase
    Gene namesi
    Name:asnO
    Ordered Locus Names:SCO3236
    ORF Names:SCE29.05c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    S.coelicolor strain A32 / MT1110 and A32 / 2377 lacking asnO produce non-hydroxylated asparagine-containing CDA variants, which are not synthesized by the wild-types but retain calcium-dependent antimicrobial activity.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 333333L-asparagine oxygenasePRO_0000350724Add
    BLAST

    Proteomic databases

    PRIDEiQ9Z4Z5.

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO3236.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 153Combined sources
    Helixi18 – 3417Combined sources
    Beta strandi35 – 373Combined sources
    Helixi42 – 5211Combined sources
    Helixi57 – 6812Combined sources
    Turni71 – 744Combined sources
    Beta strandi75 – 795Combined sources
    Turni85 – 873Combined sources
    Helixi104 – 11613Combined sources
    Beta strandi117 – 1226Combined sources
    Helixi126 – 1283Combined sources
    Beta strandi130 – 1345Combined sources
    Beta strandi152 – 1554Combined sources
    Turni157 – 1604Combined sources
    Beta strandi166 – 1749Combined sources
    Beta strandi183 – 1875Combined sources
    Helixi188 – 1914Combined sources
    Helixi192 – 1943Combined sources
    Helixi197 – 2037Combined sources
    Beta strandi208 – 2103Combined sources
    Helixi214 – 2163Combined sources
    Beta strandi228 – 2314Combined sources
    Beta strandi233 – 2386Combined sources
    Turni242 – 2443Combined sources
    Beta strandi246 – 2494Combined sources
    Helixi250 – 26617Combined sources
    Beta strandi268 – 2703Combined sources
    Beta strandi277 – 2815Combined sources
    Turni282 – 2843Combined sources
    Beta strandi285 – 2895Combined sources
    Beta strandi302 – 3109Combined sources
    Helixi312 – 3187Combined sources
    Helixi320 – 3223Combined sources
    Beta strandi324 – 3263Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OG5X-ray1.45A2-333[»]
    2OG6X-ray1.92A2-333[»]
    2OG7X-ray1.66A2-333[»]
    ProteinModelPortaliQ9Z4Z5.
    SMRiQ9Z4Z5. Positions 10-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z4Z5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the clavaminate synthase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000253609.
    InParanoidiQ9Z4Z5.
    KOiK18058.
    OMAiAHARSEY.
    OrthoDBiEOG66B3ZM.

    Family and domain databases

    InterProiIPR014503. Clavaminate_syn.
    IPR003819. TauD/TfdA-like.
    [Graphical view]
    PfamiPF02668. TauD. 2 hits.
    [Graphical view]
    PIRSFiPIRSF019543. Clavaminate_syn. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Z4Z5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAANAAGPAS RYDVTLDQSD AELVEEIAWK LATQATGRPD DAEWVEAARN
    60 70 80 90 100
    AWHAWPATLR RDLAGFRRDS GPDGAIVLRG LPVDSMGLPP TPRVNGSVQR
    110 120 130 140 150
    EASLGAAVLL MTACGLGDPG AFLPEKNGAL VQDVVPVPGM EEFQGNAGST
    160 170 180 190 200
    LLTFHNENAF HEHRPDFVML LCLRADPTGR AGLRTACVRR VLPLLSDSTV
    210 220 230 240 250
    DALWAPEFRT APPPSFQLSG PEEAPAPVLL GDRSDPDLRV DLAATEPVTE
    260 270 280 290 300
    RAAEALRELQ AHFDATAVTH RLLPGELAIV DNRVTVHGRT EFTPRYDGTD
    310 320 330
    RWLQRTFVLT DLRRSRAMRP ADGYVLGAAP QPA
    Length:333
    Mass (Da):35,982
    Last modified:May 1, 1999 - v1
    Checksum:iDE394AC07B765580
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939115 Genomic DNA. Translation: CAB38880.1.
    PIRiT36184.
    RefSeqiNP_627448.1. NC_003888.3.
    WP_003975576.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB38880; CAB38880; CAB38880.
    GeneIDi1098670.
    KEGGisco:SCO3236.
    PATRICi23736222. VBIStrCoe124346_3300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939115 Genomic DNA. Translation: CAB38880.1.
    PIRiT36184.
    RefSeqiNP_627448.1. NC_003888.3.
    WP_003975576.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OG5X-ray1.45A2-333[»]
    2OG6X-ray1.92A2-333[»]
    2OG7X-ray1.66A2-333[»]
    ProteinModelPortaliQ9Z4Z5.
    SMRiQ9Z4Z5. Positions 10-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO3236.

    Proteomic databases

    PRIDEiQ9Z4Z5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB38880; CAB38880; CAB38880.
    GeneIDi1098670.
    KEGGisco:SCO3236.
    PATRICi23736222. VBIStrCoe124346_3300.

    Phylogenomic databases

    HOGENOMiHOG000253609.
    InParanoidiQ9Z4Z5.
    KOiK18058.
    OMAiAHARSEY.
    OrthoDBiEOG66B3ZM.

    Enzyme and pathway databases

    UniPathwayiUPA00979.
    BRENDAi1.14.11.39. 5998.
    1.14.11.B11. 5998.

    Miscellaneous databases

    EvolutionaryTraceiQ9Z4Z5.

    Family and domain databases

    InterProiIPR014503. Clavaminate_syn.
    IPR003819. TauD/TfdA-like.
    [Graphical view]
    PfamiPF02668. TauD. 2 hits.
    [Graphical view]
    PIRSFiPIRSF019543. Clavaminate_syn. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.
    2. "An asparagine oxygenase (AsnO) and a 3-hydroxyasparaginyl phosphotransferase (HasP) are involved in the biosynthesis of calcium-dependent lipopeptide antibiotics."
      Neary J.M., Powell A., Gordon L., Milne C., Flett F., Wilkinson B., Smith C.P., Micklefield J.
      Microbiology 153:768-776(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN CDA BIOSYNTHESIS, DISRUPTION PHENOTYPE.
      Strain: A3(2) / 2377 and A3(2) / MT1110.
    3. "Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide."
      Strieker M., Kopp F., Mahlert C., Essen L.-O., Marahiel M.A.
      ACS Chem. Biol. 2:187-196(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH IRON AND PRODUCTS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC PARAMETERS, STEREOSELECTIVITY, REACTION MECHANISM.
      Strain: A3(2) / DSM 40783 / JCM 4979 / NBRC 15732.

    Entry informationi

    Entry nameiASNO_STRCO
    AccessioniPrimary (citable) accession number: Q9Z4Z5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 23, 2008
    Last sequence update: May 1, 1999
    Last modified: March 16, 2016
    This is version 85 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, Complete proteome, Reference proteome

    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

    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.