CPF2_COPC7
ID CPF2_COPC7 Reviewed; 542 AA.
AC A8NF99;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:31496254};
DE EC=1.14.13.196 {ECO:0000305|PubMed:31496254};
DE AltName: Full=Coprinoferrin biosynthesis cluster protein cpf2 {ECO:0000303|PubMed:31496254};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000305};
DE AltName: Full=Siderophore biosynthesis protein cpf2 {ECO:0000303|PubMed:31496254};
GN Name=cpf2 {ECO:0000303|PubMed:31496254}; ORFNames=CC1G_04211;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN [2]
RP FUNCTION.
RX PubMed=31496254; DOI=10.1021/acs.orglett.9b02861;
RA Tsunematsu Y., Takanishi J., Asai S., Masuya T., Nakazawa T., Watanabe K.;
RT "Genomic mushroom hunting decrypts coprinoferrin, a siderophore secondary
RT metabolite vital to fungal cell development.";
RL Org. Lett. 21:7582-7586(2019).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of coprinoferrin, an acylated tripeptide
CC hydroxamate siderophore (PubMed:31496254). The biosynthesis of
CC coprinoferrin depends on the hydroxylation of ornithine to N(5)-
CC hydroxyornithine, catalyzed by the monooxygenase cpf2
CC (PubMed:31496254). The second step, the acylation of N(5)-hydroxy-L-
CC ornithine to yield N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine is catalyzed
CC by a not yet identified acyltransferase (Probable). Finally, assembly
CC of coprinoferrin is catalyzed by the nonribosomal peptide synthase
CC (NRPS) cpf1 via amide bond formation between three N(5)-hexanoyl-N(5)-
CC hydroxyl-L-ornithine molecules to release the linear trimer
CC (PubMed:31496254). Interestingly, proteins seemingly not directly
CC related to biosynthesis, such as transcription factors, replication
CC factors, and autophagy-related proteins, are conserved among the
CC clusters homologous to the coprinoferrin cluster, suggesting that the
CC cluster may also play developmental and cell biological functions
CC (Probable). {ECO:0000269|PubMed:31496254, ECO:0000305|PubMed:31496254}.
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:31496254}.
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}.
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DR EMBL; AACS02000002; EAU88505.1; -; Genomic_DNA.
DR RefSeq; XP_001833232.1; XM_001833180.2.
DR AlphaFoldDB; A8NF99; -.
DR SMR; A8NF99; -.
DR STRING; 5346.XP_001833232.1; -.
DR EnsemblFungi; EAU88505; EAU88505; CC1G_04211.
DR GeneID; 6009727; -.
DR KEGG; cci:CC1G_04211; -.
DR VEuPathDB; FungiDB:CC1G_04211; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; A8NF99; -.
DR OMA; YHGNTNY; -.
DR OrthoDB; 1235295at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..542
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000452735"
FT REGION 443..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 218..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 263..266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 294..296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 518..520
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:E9QYP0"
SQ SEQUENCE 542 AA; 59780 MW; 699A4625563FB839 CRC64;
MSADDVVYDL VGLGFGPANI AIGAALTEKW QQDPTFSIKN TLFIEKHEVF RWHPGMLLPD
AKMQISFLKD LATLRTPNSP YTFLSYLHSE DRLLSFINRG STVPSRKEYS DYLAWAAQKV
QDNGVKVKFG HEIIALDDGP DGTIEVRYRN VRTQEETLIR ARDLIIAPGG TPCIPDFLQP
FVNHPRVSHS SSYALKIGDM FDSLNHLSRP LRVAIIGSGQ SAAEVTIDVR NRLASIPSTG
RHEVDMLIRK GSLKPSDDSP FANEIFDPAS TDAWFSTGSK HLRDAILAEY KQTNYSVVNP
RTLEALYEII YGQRLNAAVS RRTNVEEPSD PVINIKPYTS VLSIQTVGSQ GERVRGELLL
SPEGASASKD EGFVMVTKHM MTGAESQTNY DVILYATGYQ RTAWVELFKN TGIAKHFGIT
PSTSKVVLRP SADLVGGRQH QEFFHDSSPS TASSSTVSTP PTSPETSRFS SPISSRIVSQ
DLYLSRSYQL LPKDGENTLR PRVYLQGVEE ATHGLSDTLL SVLGVRAGEV VADLASRYHS
SA
