ID V5ENJ2_KALBG Unreviewed; 587 AA.
AC V5ENJ2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=PSEUBRA_SCAF3g04122 {ECO:0000313|EMBL:EST06640.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST06640.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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; KI545873; EST06640.1; -; Genomic_DNA.
DR RefSeq; XP_016291629.1; XM_016438059.1.
DR AlphaFoldDB; V5ENJ2; -.
DR STRING; 1365824.V5ENJ2; -.
DR GeneID; 27420737; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006937_7_0_1; -.
DR OMA; KWNSMSY; -.
DR OrthoDB; 49786at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; 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; 3.
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; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:EST06640.1};
KW Oxidoreductase {ECO:0000313|EMBL:EST06640.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377}.
SQ SEQUENCE 587 AA; 66584 MW; 1D63E32C3F117C2C CRC64;
MPDTLPPCEQ PQLTPEFHDV IIVGAGISGI AMACQLKRKL NIHDIKILER GPDPSGTWTN
NTYPGCACDV PAPVYSYSFA TKGDWSTFYP QQKELKKYFG TVAKEHDLHK NFHFQTTVNE
ARYDRDTGLW HLWSTDWTKD GEGEKHHFVC KFFVSAVGGL SQPKKCDIDG ADTFAGPIFH
TAAWDHSVDL AGKDVVLVGN GCSATQCVPY LAEHSKTLTQ FVRSKHWIAP HPHQPFDSIP
GFKWLLQRSV FVRKAQRLLI WLILESHFIM VLQNPLGRLF RWNWRRKCEA HMKKNAPREY
WDMLLPKKDE LMVGCKRRII DDDYLPTLRQ PHVKVENTKL ARIEKEHVVL ADGRKIKADV
IVMANGFEPT AAGAPMKIVG VSRTLHEHWA KYGEGGMVAY RSSLNSGFPN MGQINAANTG
TGNQSLIFAS ECTVNFLLEL AKPVLASARP PQFAIEHYPS TTLSGDQKLD LHKIPTFEVK
LKAELDEQHW IAKCMSKLVF TSGCKSWYID AKSGRVTSMQ PDWQINYMLR ATFPKWDDFR
YTGLKGGRRV PEGVPWWKRW GDWAGLGHVK YVDPKETPSI NRAAMDA
//
