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Database: UniProt
Entry: A0A074VYV6_9PEZI
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ID   A0A074VYV6_9PEZI        Unreviewed;       488 AA.
AC   A0A074VYV6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=M437DRAFT_40356 {ECO:0000313|EMBL:KEQ66005.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ66005.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ66005.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ66005.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584826; KEQ66005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074VYV6; -.
DR   STRING; 1043003.A0A074VYV6; -.
DR   HOGENOM; CLU_020931_2_0_1; -.
DR   OrthoDB; 1422935at2759; -.
DR   Proteomes; UP000030672; 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; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR   PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030672}.
SQ   SEQUENCE   488 AA;  55527 MW;  11C3EFB9FC62C1E6 CRC64;
     MSRLTQSKEQ DQAIIHDTMA PHADISEIAL ESSPERNASP WKTHLQPTPQ NDVHDVICLG
     FGPASLAIAV ALHDATKQTG KQPPQVRTQP KIGFLERQES FAWHAGMQIP GAKMQISFIK
     DMATMRNPRS EFTFLNYLHE NDRLVQFTNL STFLPRRIEF EDYLRWCAGW FQNLVSYGQE
     VVDISPDTKA KSAEGVTTWT ITSRNVHTKE LSYRRTKRVV VAVGGHPRIP DAFPQHHPRV
     VHSSQYWTLS SHIFRDRNAP LKIAVIGSGQ SAAEIFMNLP SQFPNSKAYL MIRGAALRPS
     DDSPFVNEVF DPERTDDTFG QDPETRAAAI KMDKATNYGV VRLELLEHMY DVLYTQRLTH
     GDDEEKWPQQ LLNYREVESV TDLPNDRLRL HIRNDTAKHR CRKAPTQESL DVDLVMIASG
     YRRDFHEQLL SKVRPMMPGG DKPGQKWTVN REYKVQFEPG TVAKDSGVWL QGCNESTHGV
     SLDPIFDS
//
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