SIDA_ASPOR
ID SIDA_ASPOR Reviewed; 502 AA.
AC Q2TZB2; Q8J2V1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000250|UniProtKB:E9QYP0};
DE Short=OMO {ECO:0000250|UniProtKB:E9QYP0};
DE EC=1.14.13.196 {ECO:0000269|PubMed:16233371};
DE AltName: Full=Deferriferrichrysin biosynthesis protein A {ECO:0000303|PubMed:16233371};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:16233371};
GN Name=dffA {ECO:0000303|PubMed:16233371}; ORFNames=AO090011000926;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND INDUCTION.
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16233371; DOI=10.1263/jbb.95.82;
RA Yamada O., Na Nan S., Akao T., Tominaga M., Watanabe H., Satoh T., Enei H.,
RA Akita O.;
RT "dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is
RT indispensable for deferriferrichrysin biosynthesis.";
RL J. Biosci. Bioeng. 95:82-88(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 deferriferrichrysin.
CC {ECO:0000269|PubMed:16233371}.
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:16233371};
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:16233371};
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:16233371}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:E9QYP0}.
CC -!- INDUCTION: Induced under iron-limiting conditions.
CC {ECO:0000269|PubMed:16233371}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE65353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB071287; BAC15565.1; -; Genomic_DNA.
DR EMBL; AP007171; BAE65353.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001826486.2; XM_001826434.2.
DR AlphaFoldDB; Q2TZB2; -.
DR SMR; Q2TZB2; -.
DR STRING; 510516.Q2TZB2; -.
DR PRIDE; Q2TZB2; -.
DR VEuPathDB; FungiDB:AO090011000926; -.
DR OMA; YHGNTNY; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IMP:AspGD.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..502
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000431071"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 254..257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 323..325
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 466..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 502 AA; 56941 MW; 681EC36D377B87D1 CRC64;
MEPVERKLEI GSRSYSKMPL TQQRSSGEPP RLKATPKDEL HDLLCVGFGP ASLAIAIALH
DALDPCLNKT PNSNWQPKVC FLERQKQFAW HSGMLVPGSK MQISFIKDLA TMRDPRSSFT
FLNYLHQKDR LIHFTNLSTF LPARMEFEDY MRWCAQRFAH VVSYGEEVIE VIPGKTNPSS
TLVDFFTVKS RNVETGEISA RMARKVVVAL GGTAKLPKEL PQDPRIMHSS KYCTTLPAML
KDSREAYNIA VLGSGQSAAE IFHDLQKRYP NSKTTLIMRD TAMRPSDDSP FVNEVFNPER
VDKFFSLSSA ERQRSLTADK ATNYSVVRLE LIEQIFNDMY LQRVQNPDET QWQHRILPGR
KITRVEHYGP HRRMRLHVRA VKDEKDSLVG NGKETLEVDA LMVATGYNRN AHEQLLKNVQ
HLRPAGQENW TPNREYRVEL DPSKVNAQAG IWLQGCNEQT HGLSDSLLSI LASRSGEMVN
SIFGGEFAGT TVPDTTHIRA ML
