SIDA_EMENI
ID SIDA_EMENI Reviewed; 498 AA.
AC G5EB76; C8V080; Q5B0V7; Q7Z8P5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:12828635};
DE Short=OMO {ECO:0000303|PubMed:12828635};
DE EC=1.14.13.196 {ECO:0000250|UniProtKB:E9QYP0};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000250|UniProtKB:E9QYP0};
DE AltName: Full=Siderophore biosynthesis protein A {ECO:0000303|PubMed:12828635};
GN Name=sidA {ECO:0000303|PubMed:12828635}; ORFNames=AN5823;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=WG355;
RX PubMed=12828635; DOI=10.1046/j.1365-2958.2003.03586.x;
RA Eisendle M., Oberegger H., Zadra I., Haas H.;
RT "The siderophore system is essential for viability of Aspergillus nidulans:
RT functional analysis of two genes encoding l-ornithine N 5-monooxygenase
RT (sidA) and a non-ribosomal peptide synthetase (sidC).";
RL Mol. Microbiol. 49:359-375(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the conversion of L-ornithine to N(5)-
CC hydroxyornithine, the first step in the biosynthesis of all
CC hydroxamate-containing siderophores, such as the secreted
CC triacetylfusarinine C (TAFC) involved in iron uptake and the
CC intracellular iron storage compound desferriferricrocin (DFFC).
CC {ECO:0000269|PubMed:12828635}.
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:0000269|PubMed:12828635}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- DISRUPTION PHENOTYPE: Essential for viabiliy. Grows only on
CC siderophore-supplemented growth-medium, but shows decreased
CC conidiation. {ECO:0000269|PubMed:12828635}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; AY223811; AAP56238.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70776.1; -; Genomic_DNA.
DR EMBL; AACD01000100; EAA58332.1; -; Genomic_DNA.
DR RefSeq; XP_663427.1; XM_658335.1.
DR AlphaFoldDB; G5EB76; -.
DR SMR; G5EB76; -.
DR STRING; 162425.CADANIAP00007223; -.
DR EnsemblFungi; CBF70776; CBF70776; ANIA_05823.
DR EnsemblFungi; EAA58332; EAA58332; AN5823.2.
DR GeneID; 2870942; -.
DR KEGG; ani:AN5823.2; -.
DR VEuPathDB; FungiDB:AN5823; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR InParanoid; G5EB76; -.
DR OMA; YHGNTNY; -.
DR OrthoDB; 1235295at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:AspGD.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..498
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000431072"
FT BINDING 80..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 251..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 290..293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 320..322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 463..465
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 498 AA; 56562 MW; E17627AE8BA53035 CRC64;
MEPLQRKSEL DFQSYRKMPL AQQRTQRLKP TSPEELHDLI CVGFGPASLA IAIALHDALD
PCLNKCAPTS GWQPKVAFLE RQKQFAWHSG MLVPGSRMQI SFIKDLATLR DPRSSFTFLN
YLHQKDRLIH FTNLSTFLPA RMEFEDYMRW CANQFSDVVT YGEEVIEVLP GKSSPDSPVV
DYFTVLSRNV ETGEISSRSA RKVVLALGGT AKLPAELPQD PRIMHSSKYC TALPNLLKDN
NEPYNIAVLG SGQSAAEIFH DLQKRYPNSR TSLIMRDTAM RPSDDSPFVN EVFNPERTDK
FYNLSAAERE RSLKADKATN YSVVRLELIE EIYHDMYLQR VKNPDETQWQ HRILPSRKIT
RVEHYGPNKR MRVHVRAVKD GKDSLIGDGK EVLEVDALMV ATGYNRNAHE QLLSKVQYLR
PATQDRWTPS RDYRVDLDRS KVSAGAGIWL QGSNEQTHGL SDSLLSVLAT RGGEMVESIF
GEQLESAAVP DTRFRAML
