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Protein

L-ornithine N(5)-monooxygenase

Gene

sidA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC). Highly specific for its substrate, only hydrolyzing l-ornithine. Has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate. Essential for virulence.4 Publications

Catalytic activityi

L-ornithine + NAD(P)H + O2 = N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O.2 Publications

Cofactori

FAD3 PublicationsNote: Binds 1 FAD per subunit.3 Publications

Kineticsi

kcat is 29 min(-1) with L-ornithine as substrate and 75 min(-1) with NADPH as substrate.1 Publication

  1. KM=1.7 mM for L-ornithine (in the presence of 1 mM NADH)1 Publication
  2. KM=1.7 mM for L-ornithine (in the presence of 1 mM NADPH)1 Publication
  3. KM=0.49 mM for L-ornithine (at 37 degrees Celsius)1 Publication
  4. KM=0.58 mM for L-ornithine (at 25 degrees Celsius)1 Publication
  5. KM=0.94 mM for NADPH (in the presence of 15 mM L-ornithine)1 Publication
  6. KM=0.90 mM for NADH (in the presence of 15 mM L-ornithine)1 Publication
  7. KM=4.6 µM for NADPH (at 37 degrees Celsius)1 Publication
  8. KM=2.6 µM for NADPH (at 25 degrees Celsius)1 Publication
  9. KM=18 µM for O2 (at 37 degrees Celsius)1 Publication
  10. KM=16 µM for O2 (at 25 degrees Celsius)1 Publication

    Pathway:iSiderophore biosynthesis

    This protein is involved in Siderophore biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Siderophore biosynthesis.

    Pathway:iferrichrome biosynthesis

    This protein is involved in the pathway ferrichrome biosynthesis, which is part of Siderophore biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway ferrichrome biosynthesis and in Siderophore biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021FAD; via amide nitrogen1 Publication
    Binding sitei107 – 1071Substrate1 Publication
    Binding sitei168 – 1681FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei279 – 2791NADP1 Publication
    Binding sitei323 – 3231Substrate1 Publication
    Binding sitei469 – 4691Substrate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi83 – 919FAD1 Publication
    Nucleotide bindingi254 – 2574NADP1 Publication
    Nucleotide bindingi323 – 3253NADP1 Publication
    Nucleotide bindingi466 – 4683FAD1 Publication

    GO - Molecular functioni

    • coenzyme binding Source: ASPGD
    • iron ion binding Source: ASPGD
    • monooxygenase activity Source: ASPGD
    • N,N-dimethylaniline monooxygenase activity Source: ASPGD
    • NADP+ binding Source: ASPGD

    GO - Biological processi

    • cellular iron ion homeostasis Source: ASPGD
    • cellular response to iron ion starvation Source: ASPGD
    • ergosterol biosynthetic process Source: ASPGD
    • ferrichrome biosynthetic process Source: UniProtKB-UniPathway
    • iron assimilation Source: ASPGD
    • pathogenesis Source: ASPGD
    • secondary metabolite biosynthetic process Source: ASPGD
    • siderophore biosynthetic process Source: ASPGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi1.14.13.B10. 508.
    1.14.13.B26. 508.
    UniPathwayiUPA00783.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-ornithine N(5)-monooxygenase1 Publication (EC:1.14.13.1962 Publications)
    Short name:
    OMOBy similarity
    Alternative name(s):
    L-ornithine N(5)-oxygenase1 Publication
    Siderphore biosynthesis protein A1 Publication
    Gene namesi
    Name:sidA1 Publication
    ORF Names:Afu2g07680
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530 Componenti: Chromosome 2

    Organism-specific databases

    EuPathDBiFungiDB:Afu2g07680.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Moderatley reduced growth rate during iron starvation and in iron replete conditions. Only displays 1% of wild-type conidiospore production in iron-depleted and replete conditions. Completely attenuates virulence in a mouse model of invasive pulmonary aspergillosis.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501L-ornithine N(5)-monooxygenasePRO_0000431070Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 456Combined sources
    Helixi49 – 6214Combined sources
    Turni64 – 663Combined sources
    Helixi68 – 714Combined sources
    Beta strandi79 – 879Combined sources
    Helixi92 – 943Combined sources
    Helixi105 – 1073Combined sources
    Beta strandi108 – 1103Combined sources
    Turni111 – 1133Combined sources
    Helixi121 – 1288Combined sources
    Helixi131 – 1355Combined sources
    Helixi144 – 15613Combined sources
    Helixi157 – 1615Combined sources
    Beta strandi162 – 17413Combined sources
    Beta strandi185 – 1928Combined sources
    Turni193 – 1953Combined sources
    Beta strandi198 – 20811Combined sources
    Beta strandi218 – 2203Combined sources
    Beta strandi226 – 2283Combined sources
    Helixi229 – 2313Combined sources
    Helixi232 – 2398Combined sources
    Beta strandi248 – 2525Combined sources
    Helixi256 – 26813Combined sources
    Beta strandi273 – 2775Combined sources
    Beta strandi279 – 2824Combined sources
    Helixi292 – 2965Combined sources
    Helixi300 – 3056Combined sources
    Helixi309 – 31810Combined sources
    Helixi320 – 3223Combined sources
    Turni323 – 3253Combined sources
    Helixi329 – 34517Combined sources
    Helixi349 – 3513Combined sources
    Beta strandi353 – 3575Combined sources
    Beta strandi359 – 3668Combined sources
    Beta strandi369 – 3724Combined sources
    Beta strandi374 – 3818Combined sources
    Beta strandi395 – 4039Combined sources
    Helixi412 – 4154Combined sources
    Helixi417 – 4226Combined sources
    Beta strandi436 – 4383Combined sources
    Turni442 – 4443Combined sources
    Beta strandi450 – 4534Combined sources
    Helixi458 – 4614Combined sources
    Turni463 – 4664Combined sources
    Helixi471 – 49020Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B63X-ray1.90A1-501[»]
    4B64X-ray2.28A1-501[»]
    4B65X-ray2.32A1-501[»]
    4B66X-ray2.90A1-501[»]
    4B67X-ray2.75A1-501[»]
    4B68X-ray2.29A1-501[»]
    4B69X-ray2.30A1-501[»]
    4NZHX-ray2.00A1-501[»]
    ProteinModelPortaliE9QYP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni293 – 2964Substrate binding1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000237193.
    KOiK10531.
    OMAiVWLQGCC.
    OrthoDBiEOG7C8GS3.

    Family and domain databases

    InterProiIPR025700. Lys/Orn_oxygenase.
    [Graphical view]
    PfamiPF13434. K_oxygenase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E9QYP0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MESVERKSES SYLGMRNMQP EQRLSLDPPR LRSTPQDELH DLLCVGFGPA
    60 70 80 90 100
    SLAIAIALHD ALDPRLNKSA SNIHAQPKIC FLERQKQFAW HSGMLVPGSK
    110 120 130 140 150
    MQISFIKDLA TLRDPRSSFT FLNYLHQKGR LIHFTNLSTF LPARLEFEDY
    160 170 180 190 200
    MRWCAQQFSD VVAYGEEVVE VIPGKSDPSS SVVDFFTVRS RNVETGEISA
    210 220 230 240 250
    RRTRKVVIAI GGTAKMPSGL PQDPRIIHSS KYCTTLPALL KDKSKPYNIA
    260 270 280 290 300
    VLGSGQSAAE IFHDLQKRYP NSRTTLIMRD SAMRPSDDSP FVNEIFNPER
    310 320 330 340 350
    VDKFYSQSAA ERQRSLLADK ATNYSVVRLE LIEEIYNDMY LQRVKNPDET
    360 370 380 390 400
    QWQHRILPER KITRVEHHGP QSRMRIHLKS SKPESEGAAN DVKETLEVDA
    410 420 430 440 450
    LMVATGYNRN AHERLLSKVQ HLRPTGQDQW KPHRDYRVEM DPSKVSSEAG
    460 470 480 490 500
    IWLQGCNERT HGLSDSLLSV LAVRGGEMVQ SIFGEQLERA AVQGHQLRAM

    L
    Length:501
    Mass (Da):56,877
    Last modified:April 5, 2011 - v1
    Checksum:iDD1D4DEDD2509506
    GO

    Mass spectrometryi

    Molecular mass is 57210 Da from positions 1 - 501. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY586511 Genomic DNA. Translation: AAT84594.1.
    AY819708 Genomic DNA. Translation: AAX40989.1.
    AAHF01000001 Genomic DNA. Translation: EAL93065.1.
    RefSeqiXP_755103.1. XM_750010.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00004182; CADAFUAP00004182; CADAFUAG00004182.
    GeneIDi3513640.
    KEGGiafm:AFUA_2G07680.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY586511 Genomic DNA. Translation: AAT84594.1.
    AY819708 Genomic DNA. Translation: AAX40989.1.
    AAHF01000001 Genomic DNA. Translation: EAL93065.1.
    RefSeqiXP_755103.1. XM_750010.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B63X-ray1.90A1-501[»]
    4B64X-ray2.28A1-501[»]
    4B65X-ray2.32A1-501[»]
    4B66X-ray2.90A1-501[»]
    4B67X-ray2.75A1-501[»]
    4B68X-ray2.29A1-501[»]
    4B69X-ray2.30A1-501[»]
    4NZHX-ray2.00A1-501[»]
    ProteinModelPortaliE9QYP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiCADAFUAT00004182; CADAFUAP00004182; CADAFUAG00004182.
    GeneIDi3513640.
    KEGGiafm:AFUA_2G07680.

    Organism-specific databases

    EuPathDBiFungiDB:Afu2g07680.

    Phylogenomic databases

    HOGENOMiHOG000237193.
    KOiK10531.
    OMAiVWLQGCC.
    OrthoDBiEOG7C8GS3.

    Enzyme and pathway databases

    UniPathwayiUPA00783.
    BRENDAi1.14.13.B10. 508.
    1.14.13.B26. 508.

    Family and domain databases

    InterProiIPR025700. Lys/Orn_oxygenase.
    [Graphical view]
    PfamiPF13434. K_oxygenase. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence."
      Schrettl M., Bignell E., Kragl C., Joechl C., Rogers T., Arst H.N. Jr., Haynes K., Haas H.
      J. Exp. Med. 200:1213-1219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
    2. "The Aspergillus fumigatus siderophore biosynthetic gene sidA, encoding L-ornithine N5-oxygenase, is required for virulence."
      Hissen A.H., Wan A.N., Warwas M.L., Pinto L.J., Moore M.M.
      Infect. Immun. 73:5493-5503(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
      Strain: NIH 5233 / ATCC 13073.
    3. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
    4. "Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor."
      Chocklett S.W., Sobrado P.
      Biochemistry 49:6777-6783(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, PATHWAY, SUBUNIT, MASS SPECTROMETRY.
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
    5. "Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase."
      Mayfield J.A., Frederick R.E., Streit B.R., Wencewicz T.A., Ballou D.P., DuBois J.L.
      J. Biol. Chem. 285:30375-30388(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    6. "Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase."
      Romero E., Fedkenheuer M., Chocklett S.W., Qi J., Oppenheimer M., Sobrado P.
      Biochim. Biophys. Acta 1824:850-857(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases."
      Franceschini S., Fedkenheuer M., Vogelaar N.J., Robinson H.H., Sobrado P., Mattevi A.
      Biochemistry 51:7043-7045(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD; NADP; L-ORNITHINE; LYSINE AND L-ARGININE.

    Entry informationi

    Entry nameiSIDA_ASPFU
    AccessioniPrimary (citable) accession number: E9QYP0
    Secondary accession number(s): Q4X250, Q5SE95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 26, 2014
    Last sequence update: April 5, 2011
    Last modified: July 22, 2015
    This is version 29 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, 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

    External Data

    Dasty 3

    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 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.