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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

Pathwayi

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

  1. coenzyme binding Source: ASPGD
  2. iron ion binding Source: ASPGD
  3. monooxygenase activity Source: ASPGD
  4. N,N-dimethylaniline monooxygenase activity Source: ASPGD
  5. NADP+ binding Source: ASPGD

GO - Biological processi

  1. cellular iron ion homeostasis Source: ASPGD
  2. cellular response to iron ion starvation Source: ASPGD
  3. ergosterol biosynthetic process Source: ASPGD
  4. ferrichrome biosynthetic process Source: UniProtKB-UniPathway
  5. iron assimilation Source: ASPGD
  6. pathogenesis Source: ASPGD
  7. secondary metabolite biosynthetic process Source: ASPGD
  8. siderophore biosynthetic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP, Nucleotide-binding

Enzyme and pathway databases

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: Chromosome 2

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[»]
ProteinModelPortaliE9QYP0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000237193.
KOiK10531.
OMAiFINLKTF.
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[»]
ProteinModelPortaliE9QYP0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000237193.
KOiK10531.
OMAiFINLKTF.
OrthoDBiEOG7C8GS3.

Enzyme and pathway databases

UniPathwayiUPA00783.

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: March 4, 2015
This is version 25 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.