SIDA2_COCH4
ID SIDA2_COCH4 Reviewed; 529 AA.
AC N4WYI1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:23980626};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000269|PubMed:23980626};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:23980626};
DE AltName: Full=Siderophore biosynthesis cluster protein A2 {ECO:0000303|PubMed:23980626};
GN Name=SIDA2 {ECO:0000303|PubMed:23980626}; ORFNames=COCC4DRAFT_34841;
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=23980626; DOI=10.1094/mpmi-02-13-0055-r;
RA Zhang N., MohdZainudin N.A., Scher K., Condon B.J., Horwitz B.A.,
RA Turgeon B.G.;
RT "Iron, oxidative stress, and virulence: roles of iron-sensitive
RT transcription factor Sre1 and the redox sensor ChAp1 in the maize pathogen
RT Cochliobolus heterostrophus.";
RL Mol. Plant Microbe Interact. 26:1473-1485(2013).
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:23980626). Cochliobolus
CC heterostrophus produces extracellular coprogen-type siderophores
CC including coprogen, neocoprogen I and neocoprogen II, as well as the
CC intracellular siderophore ferricrocin (PubMed:17056706). The role of
CC extracellular siderophores is to supply iron to their producers in
CC planta and the intracellular ferricrocin is required for intracellular
CC iron distribution and storage with a crucial role in ascus and
CC ascospore development (PubMed:17056706, PubMed:17601875). SIDA2
CC catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the
CC first step in the biosynthesis of all hydroxamate-containing
CC siderophores (PubMed:23980626). The assembly of extracellular coprogen-
CC type siderophores is then performed by the nonribosomal peptide
CC synthetase (NRPS) NPS6 whereas the intracellular siderophore
CC ferricrocin is assembled by NPS2 (PubMed:17056706, PubMed:17601875).
CC {ECO:0000269|PubMed:17056706, ECO:0000269|PubMed:17601875,
CC ECO:0000305|PubMed:23980626}.
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:23980626}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- INDUCTION: Expression is repressed by the transcription repressor SRE1
CC under iron replete conditions (PubMed:23980626).
CC {ECO:0000269|PubMed:23980626}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; KB733486; ENH99440.1; -; Genomic_DNA.
DR RefSeq; XP_014073320.1; XM_014217845.1.
DR AlphaFoldDB; N4WYI1; -.
DR SMR; N4WYI1; -.
DR EnsemblFungi; ENH99440; ENH99440; COCC4DRAFT_34841.
DR GeneID; 25844397; -.
DR HOGENOM; CLU_020931_2_0_1; -.
DR OrthoDB; 1235295at2759; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
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; 1.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..529
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000444391"
FT BINDING 100..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 270..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 309..312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 339..341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 493..495
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 529 AA; 59172 MW; A0EEE61C0184CE02 CRC64;
MSPHVDMSSG SPDGAAPAVQ KAFNGFLTEN IDESQFPALE NRSHLRYTPQ DELHDMICVG
FGPASLAIGV ALHDALDGTD GSLADVQGLQ SRPPKVAFLE KQPQFAWHAG MLLPGAKMQI
TFMKDMATMR NPRSEFTFLN YLHQKDRLVE FANLNTFLPA RVEYEDYMKW CASWFEEVVA
YSQEVVKVMP EKSASGEITS FNVMSHNHLT GRTESRRAKH VVIAAGGRPN IPAPFPTNHP
RVIHSSQFSY MSKQLLKDHD APYNIAVVGN GQSAAEIFDF LHANYPNSRT RLLIKGGALR
PSDDSPFVNE IFNPSRTDCT YNRAPKLRAT TLVEDKGTNY GVVRLGLLEH IYETLYMQRI
RYGNSPAEEA HWPHRILPYR RVMDVTESPV CQGGVRLHVQ DSSALYFSEQ AGGQERKETL
DVDAVFVATG YLRDLHETLL KDARHLMPGG ELEGAKWQVQ RDYRVNFTEK SVGEDAGVWL
QGCCESTHGL SDTLLSVLAT RGGEMVRSLF EKPAKWDNGH VLGGYEVRE
