ID   A0A1Y2WYC2_9PEZI        Unreviewed;       527 AA.
AC   A0A1Y2WYC2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=K445DRAFT_62504 {ECO:0000313|EMBL:OTB14663.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB14663.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB14663.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB14663.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112942; OTB14663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2WYC2; -.
DR   STRING; 1001832.A0A1Y2WYC2; -.
DR   OrthoDB; 1422935at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase 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   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57795 MW;  1335B9EA4A0773C5 CRC64;
     MAPHSLLDGH DDGPTSNGLP ENGLGVQPAR QAFNASSNNK SHLKKTPAEE VHDLVCVGFG
     PASLAVAVAL HDSINNGKLH NANTGSTPKV LFLEKQPKFA WHAGMLLPGA KMQISFIKDM
     ASLRDPTSQF TFLNYLHKNG RLVEFTNLNT FLPSRVEYED YLRWCASFFE DVVRYNSEVV
     SVSPAKGSDA NGSVSAFTVT SKDPKTGELT TYRSKNVLLA IGGQPSIPKS LPSNHPRVIH
     SSQYAHLVPQ ILNNQSSPYR VAVIGAGQSA AEIFNNIQVL YPNSRTSLIM RSEFLKPSDD
     SPFVNSIFNP SFVNSLYQRS AEERYSLLEG ARSTNYGVVR LELIERFYEK MYDQRRELGS
     DETKWPHRIM GGTDVVGFDS KGDQLRLTVR PLTSIRTAVG DVTHEDEVLE VDLVIAATGY
     QRQSHLRMIE DVAPLLPEAS EPNGAIPSSG FGRKFSEAKI NDRPVRVSRD YSVQFSPGKV
     APGSGVWLQG CCEGTHGLSD TLLSVLATRS EEIVNSIFGE GIQNGVK
//