ID V2XAM2_MONRO Unreviewed; 546 AA.
AC V2XAM2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cyclopentanone-monooxygenase {ECO:0000313|EMBL:ESK89545.1};
GN ORFNames=Moror_1205 {ECO:0000313|EMBL:ESK89545.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89545.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89545.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89545.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK89545.1}.
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DR EMBL; AWSO01000551; ESK89545.1; -; Genomic_DNA.
DR RefSeq; XP_007851154.1; XM_007852963.1.
DR AlphaFoldDB; V2XAM2; -.
DR KEGG; mrr:Moror_1205; -.
DR HOGENOM; CLU_006937_8_0_1; -.
DR OrthoDB; 1612588at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:ESK89545.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
SQ SEQUENCE 546 AA; 61224 MW; C5568AE50A01BC39 CRC64;
MSSNTQSNGR EPEFDALIVG AGFGGVYMLH NLRKAGLSVK VLEAGKDMGG VWYWNTYPGA
RVDSDLPLYQ LSDEELWKGY NWKEKFPASN EIIDYFHYVD KKLDLSRDIQ FNTQVTAAQW
DSSEDRWIIQ TEKGEAVRAR YLLLCTGIGS KPYTPSFKGL ESFKGVVHHT AGWPEGGVDF
KGKRVGVIGT GATGVQVIQE VGPVAGHLTV FQRTPNFALP MNQKQIDEAY QTKLKELYPA
YFNRRPQTFG GFYYDIVHRD TLSVSPEERI LYWEDIWAAG GFRFWVGNYG DIFTSQAAND
EAYAFWRKKV RERLTDPRMQ EKLAPTIPPH PFGTKRPSLE QNYYEIFNQP NVTLVDVNES
PIDTITEKGV KTKDGAVYEL DILLLATGYD MVTGGITQID VKGTDGVLIG DKWNDGVYTY
LGMMTANYPN MFFTYGPQGP TAFCNGPSCT EIQGQWITNL IKHAKSKGIT HIVPTRKAEE
DWRTLVHDLS NLGLWGKAKS WYMGANIPGK KVEPLNFTGG VPMYASKLQE SAEKGYEGLE
MGTVGA
//
