ID   C9SYN7_VERA1            Unreviewed;       515 AA.
AC   C9SYN7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000256|ARBA:ARBA00018612};
DE            EC=1.14.13.196 {ECO:0000256|ARBA:ARBA00012881};
DE   AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000256|ARBA:ARBA00030351};
GN   ORFNames=VDBG_10012 {ECO:0000313|EMBL:EEY23902.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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:0000256|ARBA:ARBA00001398};
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:0000256|ARBA:ARBA00001847};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
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DR   EMBL; DS985231; EEY23902.1; -; Genomic_DNA.
DR   RefSeq; XP_002999718.1; XM_002999672.1.
DR   AlphaFoldDB; C9SYN7; -.
DR   STRING; 526221.C9SYN7; -.
DR   GeneID; 9528709; -.
DR   KEGG; val:VDBG_10012; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_020931_2_0_1; -.
DR   OMA; FTNELFY; -.
DR   OrthoDB; 1422935at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR   PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:EEY23902.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EEY23902.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   REGION          27..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  57202 MW;  A31F4FACE559FB46 CRC64;
     MSTTEASEAI QSFSAFSNGG AVQNSTALNG FNGTSNGNGH TAPTQSSRAL KSNLQPTDPS
     ELHDLVLFLE KQPRFAWHAG MLLPGAKMQI SFIKDMATLR DPRSHFTFLN YLQHAGRLVE
     FTNLGTFLPS RVEYEDYLRW CASHFDDVVQ YQREVVSVSP NPQPEGAVKT FTVKSRNAKT
     GQITTVQARN VLIAAGGRPL IPKSLPAASP KVIHSSQYAH QVPKILKNTQ APYRVAVVGA
     GQSAAEIFNN VQKLYPNSKT WLVMRSEFLK PSDDSPFVNS IFNPSYTDSL YPRSQQYRRA
     LIKDAKATNY GVVRLELIEH LYEVMYDQKR EYGDDERQWP HRILNGRSIV SVNEGNHESD
     RLQLHVRRVE DSFNQSGITD EFLEQGPSSE EILDVDLIIA ATGYQRNAHV DMLRDSWNLL
     PETQPVSSGP REQVDGWEIS EGNVDSGSRK LEVGRDYKIR YAPGAIAPDA GVWLQGCCEA
     THGLSDSLLS VLAVRSGEIV DSIFPSQSKS ETSSV
//