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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

Manual assertion based on experiment ini

  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

    Pathwayi: Siderophore 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.

    Pathwayi: ferrichrome 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)DescriptionActionsGraphical viewLength
    Binding sitei102FAD; via amide nitrogen1 Publication1
    Binding sitei107Substrate1 Publication1
    Binding sitei168FAD; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei279NADP1 Publication1
    Binding sitei323Substrate1 Publication1
    Binding sitei469Substrate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi83 – 91FAD1 Publication9
    Nucleotide bindingi254 – 257NADP1 Publication4
    Nucleotide bindingi323 – 325NADP1 Publication3
    Nucleotide bindingi466 – 468FAD1 Publication3

    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
    Proteomesi
    • UP000002530 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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004310701 – 501L-ornithine N(5)-monooxygenaseAdd BLAST501

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1501
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi40 – 45Combined sources6
    Helixi49 – 62Combined sources14
    Turni64 – 66Combined sources3
    Helixi68 – 71Combined sources4
    Beta strandi79 – 87Combined sources9
    Helixi92 – 94Combined sources3
    Helixi105 – 107Combined sources3
    Beta strandi108 – 110Combined sources3
    Turni111 – 113Combined sources3
    Helixi121 – 128Combined sources8
    Helixi131 – 135Combined sources5
    Helixi144 – 156Combined sources13
    Helixi157 – 161Combined sources5
    Beta strandi162 – 174Combined sources13
    Beta strandi185 – 192Combined sources8
    Turni193 – 195Combined sources3
    Beta strandi198 – 208Combined sources11
    Beta strandi218 – 220Combined sources3
    Beta strandi226 – 228Combined sources3
    Helixi229 – 231Combined sources3
    Helixi232 – 239Combined sources8
    Beta strandi248 – 252Combined sources5
    Helixi256 – 268Combined sources13
    Beta strandi273 – 277Combined sources5
    Beta strandi279 – 282Combined sources4
    Helixi292 – 296Combined sources5
    Helixi300 – 305Combined sources6
    Helixi309 – 318Combined sources10
    Helixi320 – 322Combined sources3
    Turni323 – 325Combined sources3
    Helixi329 – 345Combined sources17
    Helixi349 – 351Combined sources3
    Beta strandi353 – 357Combined sources5
    Beta strandi359 – 366Combined sources8
    Beta strandi369 – 372Combined sources4
    Beta strandi374 – 381Combined sources8
    Beta strandi395 – 403Combined sources9
    Helixi412 – 415Combined sources4
    Helixi417 – 422Combined sources6
    Beta strandi436 – 438Combined sources3
    Turni442 – 444Combined sources3
    Beta strandi450 – 453Combined sources4
    Helixi458 – 461Combined sources4
    Turni463 – 466Combined sources4
    Helixi471 – 490Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5CKUX-ray2.10A1-501[»]
    ProteinModelPortaliE9QYP0.
    SMRiE9QYP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni293 – 296Substrate binding1 Publication4

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000237193.
    KOiK10531.
    OMAiFPSRHEF.
    OrthoDBiEOG092C38KS.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR025700. Lys/Orn_oxygenase.
    [Graphical view]
    PfamiPF13434. K_oxygenase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.

    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
    PDB 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[»]
    5CKUX-ray2.10A1-501[»]
    ProteinModelPortaliE9QYP0.
    SMRiE9QYP0.
    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.
    OMAiFPSRHEF.
    OrthoDBiEOG092C38KS.

    Enzyme and pathway databases

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

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR025700. Lys/Orn_oxygenase.
    [Graphical view]
    PfamiPF13434. K_oxygenase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 34 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

    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.