SIDA_SCHPO
ID SIDA_SCHPO Reviewed; 431 AA.
AC Q9P7T0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:15689108};
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:0000250|UniProtKB:E9QYP0};
GN Name=sib2 {ECO:0000312|PomBase:SPAC23G3.03};
GN ORFNames=SPAC23G3.03 {ECO:0000312|PomBase:SPAC23G3.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=15689108; DOI=10.1007/s10534-004-1230-z;
RA Schrettl M., Winkelmann G., Haas H.;
RT "Ferrichrome in Schizosaccharomyces pombe -- an iron transport and iron
RT storage compound.";
RL BioMetals 17:647-654(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:E9QYP0, ECO:0000305|PubMed:15689108}.
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; ferrichrome biosynthesis.
CC {ECO:0000269|PubMed:15689108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB72228.1; -; Genomic_DNA.
DR PIR; T50177; T50177.
DR RefSeq; NP_593103.1; NM_001018500.2.
DR AlphaFoldDB; Q9P7T0; -.
DR SMR; Q9P7T0; -.
DR BioGRID; 278322; 9.
DR STRING; 4896.SPAC23G3.03.1; -.
DR MaxQB; Q9P7T0; -.
DR PaxDb; Q9P7T0; -.
DR EnsemblFungi; SPAC23G3.03.1; SPAC23G3.03.1:pep; SPAC23G3.03.
DR PomBase; SPAC23G3.03; sib2.
DR VEuPathDB; FungiDB:SPAC23G3.03; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR InParanoid; Q9P7T0; -.
DR OMA; YHGNTNY; -.
DR PhylomeDB; Q9P7T0; -.
DR UniPathway; UPA00783; -.
DR PRO; PR:Q9P7T0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; TAS:PomBase.
DR GO; GO:0050661; F:NADP binding; TAS:PomBase.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; TAS:PomBase.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IGI:PomBase.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IGI:PomBase.
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 Cytoplasm; FAD; Flavoprotein; Monooxygenase; NADP; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..431
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000352807"
FT BINDING 40..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 202..205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 242..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 273..275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 399..401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 431 AA; 48582 MW; 2157A38112F4E690 CRC64;
MTEPLDLAII GFGPASLSFL IALHDHSEEP LKNKKIRVFE KLPTFSWHEG MLIPGSNMQI
SFVKDLATPR DPTSYFTFLN YLHSHGQERL SGFLNMSTLE PSRYEYHDYL CWAASHFSKF
VEYNANINKL HYDAATDLYI VGHGDTQWQA KNIIITTGCQ PYIPPLYKSV DSPLIVHSSK
FMSDHSQKLL RNSKHGILVV GCGQSAAEIW KHCHYSLDPK TPLAMCFRNL APVPSDSSPF
VNSLYFDSHN SHWWYNLPTE ARLKGLSVGR TTNYSVVKES LLEEMFKECY LQKLRYGQEF
HQIMGDTDIQ SIKNEGDHLV VQLTSQMDKS KKPETRKIDV LYVATGYDHE SFDVLMSSLF
PNSQGAQISE EYCVLNAPSK QGKVYVAGIT SNQHGIGETL LSWAAIRAGG LAKELFGPSK
PTARVPASYL N
