ID B8MJ91_TALSN Unreviewed; 470 AA.
AC B8MJ91;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=TSTA_041580 {ECO:0000313|EMBL:EED14680.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED14680.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962657; EED14680.1; -; Genomic_DNA.
DR RefSeq; XP_002484633.1; XM_002484588.1.
DR AlphaFoldDB; B8MJ91; -.
DR STRING; 441959.B8MJ91; -.
DR GeneID; 8109743; -.
DR VEuPathDB; FungiDB:TSTA_041580; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR InParanoid; B8MJ91; -.
DR OMA; FYIRESF; -.
DR OrthoDB; 1422935at2759; -.
DR PhylomeDB; B8MJ91; -.
DR Proteomes; UP000001745; 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; 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 Monooxygenase {ECO:0000313|EMBL:EED14680.1};
KW Oxidoreductase {ECO:0000313|EMBL:EED14680.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
SQ SEQUENCE 470 AA; 52904 MW; 5F920EE285971C94 CRC64;
MQSIETSSSI DAPFKASPES SQYDIVCVGF GPAALAIAIA IHERGASFDK SVLFLERQAE
FGWHTGMLLP GTKMQISFMK DLATMRNPQS YFTFVNYLHK HNRLANFINL STQTPFREEF
NDYMKWCASH FRDQVTYNQE VLNVSPGQQK APSPESAIDC FWVTSRDVQS GDVQRICSKH
VIVANGGEYS IPKGLKSPDS SDRIVHSSQY LNRVPQQFKD ENGNYNFAVV GGGQSAVEIS
EDLQSRYPKS RVSLIFRDSA LRPSDDSPFV NEIFDPASVD EFYSLDSAHR KQTLKKNKAT
NYSVVRLPLI EHIYEKIYRQ RLLKPEPRDW TLSIYNNSEV FGAKKAKSGE GLILQLRNTI
TDEVKVSEQA YDLVVLATGY HRRPFSGILK DLKPLLLSES EDNGSLVQRN YRLLFKPGSV
VRDAAIWLQG SCETTHGISD TLLSILAVRA DELLDSINAS RKTVEVKAHL
//
