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Database: UniProt
Entry: F0XQP8_GROCL
LinkDB: F0XQP8_GROCL
Original site: F0XQP8_GROCL 
ID   F0XQP8_GROCL            Unreviewed;       618 AA.
AC   F0XQP8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=CMQ_142 {ECO:0000313|EMBL:EFW99824.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFW99824.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(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; GL629807; EFW99824.1; -; Genomic_DNA.
DR   RefSeq; XP_014169239.1; XM_014313764.1.
DR   AlphaFoldDB; F0XQP8; -.
DR   STRING; 655863.F0XQP8; -.
DR   GeneID; 25974296; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006937_6_1_1; -.
DR   InParanoid; F0XQP8; -.
DR   OrthoDB; 49786at2759; -.
DR   Proteomes; UP000007796; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:EFW99824.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EFW99824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796}.
SQ   SEQUENCE   618 AA;  68328 MW;  FB3DD68D0E47015C CRC64;
     MGSVIENVPD ASIKDVVNDI LSTQVPVAQE RSINPALAAR IAARHTPKQK TWREDRPVTI
     IVIGAGIGGT TTAVLLSQKV PNATITVYDR LDKIGGTWAA NVYPGVRCDV PSHVYQLSFE
     PNLDWSEYYP KGAEIQQYYE RVVAKYGLAE RFRLGHEVVR ASWLPAASQW AVEVRSLATG
     LVSVDTADFL VSSQGRISEP KWPAIPGLAE GIFGGRTVHS ARWPADLVCE GKRVAVIGAG
     ASGQQVVSNV LRSAGHVDHY VRTKTYISSS LVGDFDEATA DAPGGHVYTD EERRTFHEEP
     GAYVSFRRDL ELRMQRRRLQ GANVIDHPAN LQLRERVVGR MLERLDGDDA WLHRITPDYV
     YGCKRPTPSP GYLEALRATP AVLSYITDSI VSIDATGIVT ADGIHRPVDV IVAATGFENG
     YTTRFPLIGL DGVDLRDRWG PDSPIGYPES YLGVMAPGYP NYFTVLQAQA NALGGSVPLQ
     AEITATYIGK AIRKLQSQSY SALDPRQDAT DDFNNLIDGF FGNKTIQGEC RSWSKIGFGK
     GRVVLAWPGS FQHRVRALRD PRWEDFRFVR RPDAAANRFE HFGNGLTDVD ESDDDVCLTS
     YLREYGELDP QRHHEYAE
//
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