SIDA_OMPOL
ID SIDA_OMPOL Reviewed; 587 AA.
AC Q52UT0;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:16019163};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000305|PubMed:16019163};
DE AltName: Full=Ferrichrome A biosynthesis protein omo1 {ECO:0000303|PubMed:16019163};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000305};
DE AltName: Full=Siderophore biosynthesis protein omo1 {ECO:0000303|PubMed:16019163};
GN Name=omo1 {ECO:0000303|PubMed:16019163};
OS Omphalotus olearius (Jack o'lantern).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Omphalotus.
OX NCBI_TaxID=72120;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=TA90170;
RX PubMed=16019163; DOI=10.1016/j.femsle.2005.06.013;
RA Welzel K., Eisfeld K., Antelo L., Anke T., Anke H.;
RT "Characterization of the ferrichrome A biosynthetic gene cluster in the
RT homobasidiomycete Omphalotus olearius.";
RL FEMS Microbiol. Lett. 249:157-163(2005).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore
CC biosynthetic pathway (PubMed:16019163). Omphalotus olearius produces
CC ferrichrome A, but no other siderophore has been detected
CC (PubMed:16019163). Ferrichrome A consists of a hexapeptide ring made up
CC of one glycine, two serine, and three N(5)-hydroxyornithine amino acid
CC residues, the latter acylated by trans-(alpha-methyl)-glutaconic acid
CC residues (PubMed:16019163). The biosynthesis of ferrichrome A depends
CC on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed
CC by the monooxygenase omo1 (PubMed:16019163). The second step, the
CC acylation of N(5)-hydroxy-L-ornithine is probably catalyzed by the N-
CC acyltransferase ato1 (PubMed:16019163). Finally, assembly of
CC ferrichrome A is catalyzed by the nonribosomal peptide synthase (NRPS)
CC fso1 (PubMed:16019163). {ECO:0000269|PubMed:16019163}.
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; ferrichrome biosynthesis.
CC {ECO:0000305|PubMed:16019163}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; AY929617; AAX49355.1; -; Genomic_DNA.
DR AlphaFoldDB; Q52UT0; -.
DR SMR; Q52UT0; -.
DR UniPathway; UPA00783; -.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:UniProtKB-UniPathway.
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.
FT CHAIN 1..587
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000444314"
FT REGION 488..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 235..238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 282..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 312..314
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 567..569
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 570
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 587 AA; 64105 MW; 5F9907EC863C040F CRC64;
MSQMSITSQV IYDLVGLGFG PSNVAIAGAL VDKWASPNSD AKSRSFQNVL FIEKHTSFQW
HPGMLIPGAQ MQISFLKDLA TLRSPQSPIT FLNYLHSQNR LASFINRGST TPSRKEYADY
LGWAARYVQD HGVKVNYGQE VIAIDEDADG LIGITSKDVT TNEIYTYKTR NLVISPGGSP
RIPLTIAPLM NEPSVINDST VLHSSAYLTS VDRLFQSLTR SSSSRRPFKI AVVGGGQSAA
EVSLNLRERL SSIAFEGSVG HQVDMIIGRG SLKPSDDTPF SNEVFDPMTT DTWFGSSQHN
RDRMITEYKP TNYSVVNPRT INAVRHVSPS LIYDQKVDDA IAARTLEDKT SGTSPARINI
RANMRIVSLK YDDKNSTDSS SSPTTKSSSA FTLTLQNTHT PHTLHASAYD AIICATGYQR
TGWIDMFKRS KRLGKHFGIG AEGAARVKLV PLDKRQRVDV DTLFDETAIS SDVSSTASSS
LYSVSGSDNS AASGVSGAST PLTSPSEEEG KSDVNLYISR RYRLLPVSTS SYEKTKTRDD
DASEGVKMKA RIYVQGVEEM THGLSDTLLS VIGPRAGEVV EDLFAEE
