ID A0A1J9SK90_9PEZI Unreviewed; 494 AA.
AC A0A1J9SK90;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BKCO1_2000212 {ECO:0000313|EMBL:OJD40021.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD40021.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD40021.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD40021.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD40021.1}.
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DR EMBL; MNUE01000002; OJD40021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9SK90; -.
DR STRING; 236234.A0A1J9SK90; -.
DR OrthoDB; 1422935at2759; -.
DR Proteomes; UP000183809; 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:UP000183809}.
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 55720 MW; E7A31F24602F7FC3 CRC64;
MSPHAEYAAP PQNNNQPLRS VHRATQPKMH RNTSYLRPSS EDELHDILCV GFGPASLAIA
VAMHDAIEAS GHVGQLDRLP KVAFLEKQPE FRWHAGMLLE GAHMQISFIK DMATLRNPRS
NFTYLNYLHK NDRLIDFTNL STFLPPRDEY EDYLRWCASH FDDVASYGQE VVQVVPEKTT
IDSAAVDAFV VKSRNIVTGE TTSRRARHVV IATGGRAKIP EPFPKDHARV IHSSAFKYTA
PKLLRERNAP YKIAVIGGGQ SAAEIFENLQ SNYPNSSTNL IIRGQHLRPS DDSPFVNEIF
NPERTDDMFS RDADLRTKTI LDDKVTNYGV VRLNLLERIF ETMYLQKMRY GAQENWPHRI
LNFRTIVDAG ESPVIKGGVR LVVNNHSNEF CAQKSATEEV HDYDLVVVAV GYERNEHEDI
LQGSRWLMPG GGSAGQKWEV NRQYGVLFEE GKVSNNAGIW LQGCNEMTHG VSLPRPLLMF
FSPIPRATSL PSIL
//
