ID A0A1J9S5J4_9PEZI Unreviewed; 535 AA.
AC A0A1J9S5J4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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_2000067 {ECO:0000313|EMBL:OJD34877.1};
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:OJD34877.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD34877.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD34877.1,
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:OJD34877.1}.
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DR EMBL; MNUE01000020; OJD34877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9S5J4; -.
DR OrthoDB; 5491437at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
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; PTHR38663; -; 1.
DR PANTHER; PTHR38663:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809}.
SQ SEQUENCE 535 AA; 60427 MW; 932EBEEEBBC2633C CRC64;
MDSPTRENSI FVHDVIIIGA GPCGLAVAAR LCEHTPSAIF TDEEHQRYHW IRKHGASMSI
KNWKNGQVTQ AAPRLGRRYS TLVLDGSGDQ WLSRWNRLFK TFEITNLRSP MFWHVDPCDR
DGLLAYTYEQ RRENELIEIR ECVGKEVSKH LRKKRTKSRK AHSEVEVDER DRKDYFRPSR
LLFAEHCECI ADRYGLRDGL IKQEQVQDIE YGCVRDVSDV DKIFTLRTNN GAYHARTVVL
AVGPANAPSL PNIDPKQGCP QMCHAMQIQQ FPDPIVSAKL KAKKETNVLV VGGGLTSAQV
SDMAVRKGVT KVWHLMRSGC KVKPFDVDLA WMGKFRNIEQ AIFWSADTDE ERLEQIKAAR
GGGSITPPFH KILKQHMARG RVALHTHTVI KSKSYDASTQ TWMVNTDPPI PELPPIDYIY
FSTGIQTDFQ TLPCLQSMNR DYPIHGHGGL PCLNDDLMWK DDVPLFVTGR LAGLRLGPAA
GNLGGARTGA ERIAWSIEDV LAKSREVVEE NDEDFDYVTA RGNRYTSLSA VDIDE
//