SIDA_USTMA
ID SIDA_USTMA Reviewed; 649 AA.
AC P56584; A0A0D1E2N5; Q4P3Z9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
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:0000250|UniProtKB:E9QYP0};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:8430103};
GN Name=SID1; ORFNames=UMAG_10188;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=518;
RX PubMed=8430103; DOI=10.1073/pnas.90.3.903;
RA Mei B., Budde A.D., Leong S.A.;
RT "sid1, a gene initiating siderophore biosynthesis in Ustilago maydis:
RT molecular characterization, regulation by iron, and role in
RT phytopathogenicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:903-907(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 ferrichrome.
CC {ECO:0000269|PubMed:8430103}.
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:8430103};
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:8430103};
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:0000269|PubMed:8430103}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M98520; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M98523; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M98523; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M98520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003143; KIS70091.1; -; Genomic_DNA.
DR PIR; A47266; A47266.
DR RefSeq; XP_011388351.1; XM_011390049.1.
DR AlphaFoldDB; P56584; -.
DR SMR; P56584; -.
DR STRING; 5270.UM05164P0; -.
DR EnsemblFungi; KIS70091; KIS70091; UMAG_10188.
DR GeneID; 23566252; -.
DR KEGG; uma:UMAG_10188; -.
DR VEuPathDB; FungiDB:UMAG_10188; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; P56584; -.
DR OrthoDB; 1235295at2759; -.
DR BioCyc; MetaCyc:MON-18961; -.
DR UniPathway; UPA00783; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
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 Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..649
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000204035"
FT REGION 512..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 289..292
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 314
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 328..331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 359..361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 569..571
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 572
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 649 AA; 71531 MW; C0B5434239FDE088 CRC64;
MSAPTLDVES PLAASTSSLR AMNMVSSHTT VAKDEIYDLL GIGFGPAHLA LSISLRESSE
ANETNFKAHF LEKRGHFAWH PALLLPGSQL QVSPLKDLVT LRDPASTYSF YNYLHSHGRL
ARYINKEQGV PSRREWTSYL AWAARRMNQA VSYGQDVISI EPLALASASP DAKQDTVAVR
PASAQEADSL CLYQVRIRDE STGHIVNRYA RNLSVAVGGV PKLPPAFQAA WDEQQRAPHS
IPRLVHSGFY IPSMLKLEPE LHKAASLRHP DAAAQLDDSS RLRLAVIGAG QSSTEMFMNL
HSRFPSAIVT MIFRASALVP SDDTGFVNSA AFDPERTDEF WQASETQRRK WLQEFKRTNY
SVVRTDLLNE LHDAMYDKYE VQLPEELQDP TEKQAGRMEM RRCTEVVEVT PLDDGIQLTM
RDNLRNAKLE TIRFDAVFLG TGFIRSPSKM RFLEQLKPFY PALDAEWMSR DTIAEEDEVS
KSIDVEDEEV IERRREMLRG ITRDYRLVPA SAMQSDAVRS GKSSPGSGSD ASSTSSQQTL
ASENSTENLP EASLYVLGGN EATHGLSDSL LSIVAHRAGE LTTSLLQRLP RTRRGTASSA
ATQPAASTVA SAAKTSPTVS VTQTKARQAA QVVNDKLAAL SGLHLDATS
