ID   SIDA_CERS8              Reviewed;         541 AA.
AC   M2PP75;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:28842536};
DE            EC=1.14.13.196 {ECO:0000305|PubMed:28842536};
DE   AltName: Full=Basidioferrin biosynthesis protein SMO1 {ECO:0000303|PubMed:28842536};
DE   AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000305};
DE   AltName: Full=Siderophore biosynthesis protein SMO1 {ECO:0000303|PubMed:28842536};
GN   Name=SMO1; ORFNames=CERSUDRAFT_113443;
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B;
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
RN   [2]
RP   INDUCTION, AND FUNCTION.
RC   STRAIN=B;
RX   PubMed=28842536; DOI=10.1128/aem.01478-17;
RA   Brandenburger E., Gressler M., Leonhardt R., Lackner G., Habel A.,
RA   Hertweck C., Brock M., Hoffmeister D.;
RT   "A highly conserved basidiomycete peptide synthetase produces a trimeric
RT   hydroxamate siderophore.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
CC   -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore
CC       basidioferrin biosynthetic pathway (PubMed:28842536). The biosynthesis
CC       of basidioferrin depends on the hydroxylation of ornithine to N(5)-
CC       hydroxyornithine, catalyzed by the monooxygenase SMO1
CC       (PubMed:28842536). The second step, the acylation of N(5)-hydroxy-L-
CC       ornithine is catalyzed by a not yet identified N-acyltransferase
CC       (PubMed:22434909). Finally, assembly of basidioferrin is catalyzed by
CC       the nonribosomal peptide synthase (NRPS) NPS2 via amide bond formation
CC       between three L-AHO molecules to release the linear L-AHO trimer
CC       (PubMed:22434909). {ECO:0000269|PubMed:28842536}.
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:0000250|UniProtKB:E9QYP0};
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:0000250|UniProtKB:E9QYP0};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:E9QYP0};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9QYP0};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:28842536}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC   -!- INDUCTION: Expression is induced under iron-depleted conditions
CC       (PubMed:28842536). {ECO:0000269|PubMed:28842536}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB445795; EMD38274.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2PP75; -.
DR   SMR; M2PP75; -.
DR   STRING; 914234.M2PP75; -.
DR   EnsemblFungi; EMD38274; EMD38274; CERSUDRAFT_113443.
DR   HOGENOM; CLU_020931_2_0_1; -.
DR   OrthoDB; 1235295at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
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; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR42802; PTHR42802; 2.
DR   Pfam; PF13434; K_oxygenase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..541
FT                   /note="L-ornithine N(5)-monooxygenase"
FT                   /id="PRO_0000444313"
FT   REGION          430..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50..58
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         69
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         223..226
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         269..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         300..302
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         520..522
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT   BINDING         523
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ   SEQUENCE   541 AA;  59598 MW;  B92BACBB57F12F77 CRC64;
     MEAQDPLFDL IGLGFGPANL AIAGAIVEKW EGPSAGGDGG ISAHKVLFIE KQPEFQWHPG
     MLLPNTRMQI SFLKDLATLR SPQSPLTFLS YLHAEGRLLP FINRGSFTPT RREYFDYLSW
     AARTVESKGI KVQYGEEVVS IRGSEDNTVE VHSRDVKTGT IVIRRTRNLV ISPGGNPKLP
     PNISLLYPHP RILHSSRYAT SVDQLLGTLS PANRPLRIAV IGSGQSAAEV TLDLHSRLSS
     MPGGDRPHAI DMIFRNGSLK PSDDSPFSNE IFDPDTTEVI YNLPTQSDRE NILKEYNNTN
     YSVVNPRTID AMYEVMYDQK LDDAIARRKG DKATPSAARI TMHPHMTLYF ADDLPQLAET
     DSATETSQEG IRLTLQNVFS QAQSTRDYDA VVCATGYDRT SWLRMLTSSD IGKHFGLNLS
     SDPVQLVPST EIPKGPDGSL FDASEEEATW RPASPITPAS PSPPSTPTSS ALSQSRMLGQ
     LPITKLYITR EYCLVPNSPQ FKPRIYLQGC TEATHGLSES LLSILGVRAG LVVDDLWKNS
     Q