SIDA_GIBZE
ID SIDA_GIBZE Reviewed; 536 AA.
AC I1RN13;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:20507510};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000305|PubMed:20507510};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:20507510};
DE AltName: Full=Siderophore biosynthesis protein A {ECO:0000303|PubMed:20507510};
GN Name=SID1 {ECO:0000303|PubMed:20507510};
GN ORFNames=FG05371, FGRAMPH1_01T17749;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION.
RX PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA Turgeon B.G.;
RT "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT mediated iron metabolism, is a conserved virulence determinant of plant
RT pathogenic ascomycetes.";
RL Plant Cell 18:2836-2853(2006).
RN [5]
RP FUNCTION.
RX PubMed=17043871; DOI=10.1007/s00294-006-0103-0;
RA Tobiasen C., Aahman J., Ravnholt K.S., Bjerrum M.J., Grell M.N., Giese H.;
RT "Nonribosomal peptide synthetase (NPS) genes in Fusarium graminearum, F.
RT culmorum and F. pseudograminearium and identification of NPS2 as the
RT producer of ferricrocin.";
RL Curr. Genet. 51:43-58(2007).
RN [6]
RP FUNCTION.
RX PubMed=17601875; DOI=10.1128/ec.00111-07;
RA Oide S., Krasnoff S.B., Gibson D.M., Turgeon B.G.;
RT "Intracellular siderophores are essential for ascomycete sexual development
RT in heterothallic Cochliobolus heterostrophus and homothallic Gibberella
RT zeae.";
RL Eukaryot. Cell 6:1339-1353(2007).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20507510; DOI=10.1111/j.1364-3703.2007.00401.x;
RA Greenshields D.L., Liu G., Feng J., Selvaraj G., Wei Y.;
RT "The siderophore biosynthetic gene SID1, but not the ferroxidase gene FET3,
RT is required for full Fusarium graminearum virulence.";
RL Mol. Plant Pathol. 8:411-421(2007).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of hydroxamate-containing siderophores that
CC play a critical role in virulence (PubMed:20507510). Gibberella zeae
CC produces extracellular coprogen-type siderophores as well as the
CC intracellular siderophore ferricrocin (PubMed:17056706). The role of
CC extracellular siderophores is to supply iron to the fungus during plant
CC infection, and the intracellular ferricrocin is required for
CC intracellular iron distribution and storage with a crucial role in
CC ascus and ascospore development (PubMed:17056706, PubMed:17043871,
CC PubMed:17601875). SID1 catalyzes the conversion of L-ornithine to N(5)-
CC hydroxyornithine, the first step in the biosynthesis of all
CC hydroxamate-containing siderophores (PubMed:20507510). The assembly of
CC extracellular coprogen-type siderophores is performed by the
CC nonribosomal peptide synthetase (NRPS) NPS6 whereas the intracellular
CC siderophore ferricrocin is assembled by NPS2 (PubMed:17056706,
CC PubMed:17043871, PubMed:17601875). {ECO:0000269|PubMed:17043871,
CC ECO:0000269|PubMed:17056706, ECO:0000269|PubMed:17601875,
CC ECO:0000269|PubMed:20507510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000250|UniProtKB:E9QYP0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NAD(+); Xref=Rhea:RHEA:41512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000250|UniProtKB:E9QYP0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E9QYP0};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9QYP0};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:20507510}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- INDUCTION: Expression is induced under iron starvation conditions
CC (PubMed:20507510). {ECO:0000269|PubMed:20507510}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of siderophores and leads
CC to slow growth under low iron conditions (PubMed:20507510). Does not
CC affect the ability to infect single, inoculated spikelets, but unables
CC the spreading from spikelet-to-spikelet through the rachises of wheat
CC spikes (PubMed:20507510). {ECO:0000269|PubMed:20507510}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF88195.1; -; Genomic_DNA.
DR RefSeq; XP_011323895.1; XM_011325593.1.
DR AlphaFoldDB; I1RN13; -.
DR SMR; I1RN13; -.
DR STRING; 5518.FGSG_05371P0; -.
DR GeneID; 23552556; -.
DR KEGG; fgr:FGSG_05371; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17749; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR InParanoid; I1RN13; -.
DR PHI-base; PHI:1010; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802; PTHR42802; 2.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..536
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000444438"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 286..289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 355..357
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 517..519
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 536 AA; 59299 MW; 88914D0BD4FB3644 CRC64;
MSPHSEISFS GSDAAVSNGT SNGINGHSNG TNGFSNGHMN GHSNGNDAPT AVRHGPRVHK
ERSRHLETAP VDSEFDLICA GFGPASLAVA VAMHDAIAEG RNLRPDGTAP KVLFLEKQPK
FAWHAGMLLP GAKMQISFIK DMATLRNPRS EFTFLNYLHS QGRLVDFTNL GTFLPARTEY
EDYLRWCSSW FDHVVNYNNE VLSISPENKE AGAVKTFTVQ ARNGKTGQIQ SFRSRHVLVA
AGGQPSLPKS LPAKHPRVLH SSQFANYAPQ ILTKQNAPYR VAVIGAGQSA AEIFNNVQNL
YPNSKTYLIM RQEFLRPSDD SPFVNSIFNP EYIDNLWPRS VKARETLLTE ARATNYGVVR
LELIEHLFEK MYDQKREISD DETQWPHRIL SGREIASVDT KGDALEIKVQ RVNDGPLDGF
VDQETFDVDL IIAATGYKRS AHIDMLKDAW TMLPKTVSGR NESPKGANGW NVETQDGERK
LAVARDYRVK FSPGTVADDS GVWLQGCCEG THGLSDTLLS VLSTRSGEIV QSIFKQ
