ID A0A168CQP8_CORDF Unreviewed; 537 AA.
AC A0A168CQP8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=LEL_08908 {ECO:0000313|EMBL:OAA71673.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA71673.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA71673.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA71673.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA71673.1}.
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DR EMBL; AZHF01000008; OAA71673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168CQP8; -.
DR OrthoDB; 5491437at2759; -.
DR Proteomes; UP000076881; 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; PTHR38663; -; 1.
DR PANTHER; PTHR38663:SF1; ZGC:113276; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
SQ SEQUENCE 537 AA; 60161 MW; F486FB3C6AE89605 CRC64;
MDNQDIKDVI IIGGGVCGLA MAARLREQTP SALFTDEEHR RFRWIGKHGN KVSLKQTKSG
KIKTRRPSTG PGYNMLVLDS TDDQWLARWH YLFHTYEISH LRSPMLWHAD PFDRDSLLAY
TYENKREDEL VEIRNCVGKE VSKHGHKKAA GRHCGGKQTS RVAINVRDKN DYFTPSCGVF
RDHCASVTQR YDLEAGVLQK EAVQNLDFGY VETFPDEPEK LFTVTTDNGV RYARTVVMAV
GAANAPKVPV IPSMPNANGQ YPQACHSLQI KEFPDPYLRS RIKAKQATNV VVVGGGLTSA
QLTDLAIRRG VTRVWHIMRG PCRVKLFDLS LEWMGKYKNT EQARFWLADS DEERLDIIKT
ARGGGSITPL YNKILKKHIA AGKVELITNT SIVDARFEPR AGQDGGQWHI TTNPPVELPP
MDFMYFATGI QTDFTSLPYM QTILRKHPVQ GFGGFPCLND DLMWSDDVPL FMVGRLAALR
LGPGAANIGG AMVGAERVSW AIEDILRRSQ PEAESDSPAM EEYLKGHSNM YSTLACE
//
