ID M3D1K8_SPHMS Unreviewed; 579 AA.
AC M3D1K8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cyclododecanone monooxygenase {ECO:0000313|EMBL:EMF11383.1};
GN ORFNames=SEPMUDRAFT_68932 {ECO:0000313|EMBL:EMF11383.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11383.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11383.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11383.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB456266; EMF11383.1; -; Genomic_DNA.
DR RefSeq; XP_016759504.1; XM_016909845.1.
DR AlphaFoldDB; M3D1K8; -.
DR GeneID; 27906982; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006937_8_2_1; -.
DR OMA; ALKPWYG; -.
DR OrthoDB; 2785305at2759; -.
DR Proteomes; UP000016931; 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:SF4; BLR3857 PROTEIN; 1.
DR PANTHER; PTHR43098; 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:EMF11383.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
SQ SEQUENCE 579 AA; 66228 MW; CFBD0CDFF8C5C74A CRC64;
MEAQKKYDAE REKRLAFGRD ISQYRVVDGH FASWLGDPWK AETPREPVYR ETDVLIMGGG
YGSQLTAAEL LKYGIQNFLM VDKCGGFGGT WWWNRYPGAQ CDIESFIYMP LLEETGYVPT
EKYAHQPELL EHAERIATHY GLHEKALFQT EILSIHWEEY KGVWRIITNH NDTIYARFVV
LNSGPLHRPK LPGTPGIEKF KGHAFHSSRF DYEYCGKDLS KLQDKKVAII GTGATAVQII
PHVAKNAKEF FVVQRTPSGV DTRLNCDTTE EWIKENIKPG WQKNRQHNFN KMSLGGATDE
DLVDDNWSRV FLSFTNATKG AKPEDIPREI LRKNFERMQS IRDRVDSTIQ DPKVAEKLKP
WYGWGCKRPT FHDGYLPSFN RPNVHLIDTD GKGIDEFTET GFKFNGVEYE VDAVIFATGY
ELATDWVQRA GMDVYGRSEP ISKKWANGTI GLHSWGSNGF PNAFWITTAQ GPLAVNALYG
IHEQAIHLSY IINETLRRGA KCVEPSKEAE EAWLKEVLKA GQNRSTFEAT CTPGWMNNEG
HVTEKHVRNW WYGGNGLEYF KMIKDWRDAG KLEGLKVTY
//
