SIDA_AJECA
ID SIDA_AJECA Reviewed; 475 AA.
AC B2KWI1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:18404210};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000269|PubMed:18404210};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:18404210};
DE AltName: Full=Siderophore biosynthesis cluster protein 1 {ECO:0000303|PubMed:18404210};
GN Name=SID1 {ECO:0000303|PubMed:18404210};
GN Synonyms=LOM1 {ECO:0000303|PubMed:16030248};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18404210; DOI=10.1371/journal.ppat.1000044;
RA Hwang L.H., Mayfield J.A., Rine J., Sil A.;
RT "Histoplasma requires SID1, a member of an iron-regulated siderophore gene
RT cluster, for host colonization.";
RL PLoS Pathog. 4:E1000044-E1000044(2008).
RN [2]
RP INDUCTION.
RX PubMed=16030248; DOI=10.1091/mbc.e05-05-0434;
RA Nittler M.P., Hocking-Murray D., Foo C.K., Sil A.;
RT "Identification of Histoplasma capsulatum transcripts induced in response
RT to reactive nitrogen species.";
RL Mol. Biol. Cell 16:4792-4813(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21341981; DOI=10.3109/13693786.2011.558930;
RA Hilty J., George Smulian A., Newman S.L.;
RT "Histoplasma capsulatum utilizes siderophores for intracellular iron
RT acquisition in macrophages.";
RL Med. Mycol. 49:633-642(2011).
RN [4]
RP INDUCTION.
RX PubMed=22117028; DOI=10.1128/ec.05274-11;
RA Hwang L.H., Seth E., Gilmore S.A., Sil A.;
RT "SRE1 regulates iron-dependent and -independent pathways in the fungal
RT pathogen Histoplasma capsulatum.";
RL Eukaryot. Cell 11:16-25(2012).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of hydroxamate-containing siderophores that
CC play a critical role in virulence via intracellular iron acquisition
CC during macrophage infection (PubMed:18404210, PubMed:21341981). SID1
CC catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the
CC first step in the biosynthesis of all hydroxamate-containing
CC siderophores (PubMed:18404210). {ECO:0000269|PubMed:16030248,
CC ECO:0000269|PubMed:18404210}.
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:0000269|PubMed:18404210};
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:0000269|PubMed:18404210};
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. {ECO:0000269|PubMed:18404210}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- INDUCTION: Expression is induced during iron deprivation
CC (PubMed:18404210). Also induced in response to reactive nitrogen
CC species (PubMed:16030248). Expression is regulated by the transcription
CC factor SRE1 (PubMed:22117028). {ECO:0000269|PubMed:16030248,
CC ECO:0000269|PubMed:18404210, ECO:0000269|PubMed:22117028}.
CC -!- DISRUPTION PHENOTYPE: Results in poor growth under low iron conditions
CC and loss of siderophore production (PubMed:18404210, PubMed:21341981).
CC Leads also to a significant growth defect in human and murine
CC macrophages and attenuation in the mouse model of infection
CC (PubMed:18404210, PubMed:21341981). {ECO:0000269|PubMed:18404210,
CC ECO:0000269|PubMed:21341981}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; EU253976; ACC64454.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KWI1; -.
DR SMR; B2KWI1; -.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802; PTHR42802; 1.
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..475
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000444390"
FT BINDING 65..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 238..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 277..280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 307..309
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 446..448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 475 AA; 53388 MW; B79004CAABDD5E7A CRC64;
METVLKNDCS HCQESVILRE NGGAGRSSNT GIQHDIICVG FGPAALAIAI AMRDRGIQRR
VRFLERQPEF GWHTGMLLPG SKMQISFIKD LATIRNPRSH FTFLNYLHQK DRLVHFTNLS
THLPFREEFN DYMKWCASHF NDWVQYNQEV LSVTAVESTP GRPAEYFKLI SRDVRSGELR
ELSANHIIVA SGGEPAIPPI LSTQHLPKTV IHSSTYLGSV HHLLQEKNGS YRFAVVGGGQ
SAVEISEDIQ SRYANSKVTL VTKASALKPS DDSPFVNEIF DPSSVDKFYS LDHSARQQTL
LENKATNYGV VRLPLLESVY EKLYRQKFLE PNPAKWPFRL VTGREVMGLK ELPNNQIELQ
LKDTLSGRVE SSAEVYDLVI LATGYTRNPI ATMLKPLEQI VEAPADGKTY CTDRDYRLRF
RQGKVKRDAG IWLQGCCESS HGLSDSLLSI LAVRSSELLD SILASSKRAE DHARL
