SIDA_ARTBC
ID SIDA_ARTBC Reviewed; 501 AA.
AC D4AU57;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:26960149};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000305|PubMed:26960149};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:26960149};
DE AltName: Full=Siderophore biosynthesis protein A {ECO:0000303|PubMed:26960149};
GN Name=sidA {ECO:0000303|PubMed:26960149}; ORFNames=ARB_07687;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=26960149; DOI=10.1371/journal.pone.0150701;
RA Kroeber A., Scherlach K., Hortschansky P., Shelest E., Staib P.,
RA Kniemeyer O., Brakhage A.A.;
RT "HapX mediates iron homeostasis in the pathogenic dermatophyte Arthroderma
RT benhamiae but is dispensable for virulence.";
RL PLoS ONE 11:E0150701-E0150701(2016).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore
CC biosynthetic pathway (PubMed:26960149). Arthroderma benhamiae produces
CC 2 types of extracellular siderophores, ferrichrome C and ferricrocin
CC (PubMed:26960149). The biosynthesis of these siderophores depends on
CC the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by
CC the monooxygenase sidA (PubMed:26960149). The structure of ferricrocin
CC differs from ferrichrome C only by a serine for alanine substitution
CC and the assembly of both siderophores is suggested to be performed by
CC the nonribosomal peptide synthase (NRPS) sidC (PubMed:26960149).
CC {ECO:0000269|PubMed:26960149}.
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. {ECO:0000305|PubMed:26960149}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- INDUCTION: Expression is under the control of the iron acquisition
CC regulator hapX (PubMed:26960149). {ECO:0000269|PubMed:26960149}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; ABSU01000010; EFE33327.1; -; Genomic_DNA.
DR RefSeq; XP_003013967.1; XM_003013921.1.
DR AlphaFoldDB; D4AU57; -.
DR SMR; D4AU57; -.
DR STRING; 663331.D4AU57; -.
DR EnsemblFungi; EFE33327; EFE33327; ARB_07687.
DR GeneID; 9521385; -.
DR KEGG; abe:ARB_07687; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR OMA; YHGNTNY; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..501
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000444389"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92..100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 263..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 304..307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 334..336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 476..478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 501 AA; 56173 MW; 9962DD538966B78D CRC64;
MNGTSTTGNG FTNGTNYPVP KLELQPETTS TSPTRAQTHP LLPSVSDDEL HDLICVGFGP
ASLAIAIALH DRLLETAHSP DITTVPKICF LEKQSNFAWH SGMLLPGSKM QISFIKDLAT
IRNPRSEFTF LNYLQVHDRL LDFANLGTFL PARIEFEDYM KWCASKFANL VRYRTEVLDV
TPSEVDPVTG KVHFFTVRSK VLETGEVTTR KARHVVVAIG GKPNIPAEFP TNSRIIHSSA
YCTTLPSLLN NTLKEYSIAV AGSGQSAAEI FHDLQKRYPN AKTSLIMRDS ALRPSDDSPF
PSVNELFNPE RVDQFFNQSE KERQHFLERH RSTNYSVVRP ELIEQIYADM YIQKIQYPDE
TQWQHRIFSS CLISKVDSDK SEKLNLSLQH CHSENTTMNG THNEEMNADA LILATGYVRN
AHESILASIE PLLAQKHMGW KVQRNYRLEL DKNQVDVDAG IWLQGCNEST HGLSDSLLSI
LAVRGAEIVQ AIFGAQISNG N
