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Database: UniProt
Entry: A0A2A9NT85_9AGAR
LinkDB: A0A2A9NT85_9AGAR
Original site: A0A2A9NT85_9AGAR 
ID   A0A2A9NT85_9AGAR        Unreviewed;       571 AA.
AC   A0A2A9NT85;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=AMATHDRAFT_478 {ECO:0000313|EMBL:PFH54195.1};
OS   Amanita thiersii Skay4041.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX   NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH54195.1, ECO:0000313|Proteomes:UP000242287};
RN   [1] {ECO:0000313|EMBL:PFH54195.1, ECO:0000313|Proteomes:UP000242287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKay4041 {ECO:0000313|EMBL:PFH54195.1,
RC   ECO:0000313|Proteomes:UP000242287};
RG   DOE Joint Genome Institute;
RA   Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA   Pringle A.;
RT   "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT   fungi.";
RL   Submitted (FEB-2014) 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}.
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DR   EMBL; KZ301970; PFH54195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9NT85; -.
DR   STRING; 703135.A0A2A9NT85; -.
DR   OrthoDB; 49786at2759; -.
DR   Proteomes; UP000242287; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  64637 MW;  266DC258878A5C75 CRC64;
     MAGHSTRSTP TLSKSPMASR DGKRTPLVII VGAGLAGIST AIALRRQLQF ENFIIYEKAD
     DVGGTWRDNT YPGCGSDVPG HWYSLSTDLN PYWSTYYISQ PEIQAYWVEL WHKYGLKSRT
     KLGHAVRSAE WDTRRQLYKI QVEKVATGEV FETEAEVMFY AIGGFMSPVY PKDVAGVEVF
     HGDAWHSARW NHNVDLKGKR VGVIGNGCSA AQFVPEIAAE PSISVVNFVR TPQWYVPREN
     FKYPRWLQWV FAHVPFVMRC YRNLIMARSD LMFLIFRKSN KRILALTRRM FAAYIKKVAP
     KDQLEKLIPT YSPGCKRIIV DPGYLKCLHQ PNVNLRWEGI DSIVEEGIKL KTGEIVPLDV
     IIFGTGYSLE PADITIRGRK GKTMREYDNE HGGAAAYAGS CRPGFPNLFT LLGPNVASGH
     ASVIFSEEAQ VKKRSGQIRD VLLTVALQIN HALQLIKPIL DGQAKSFEVK EDVCDEYDGW
     VQKRLKTSVW MECNSYYQVG GNNETKNVAT FPGPVSLFWW LIRTPDWSKF DGVGKEEWER
     VRRMETLRRV GLVGMGLALA MSMRILGSKF K
//
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