ID K1XSI3_MARBU Unreviewed; 338 AA.
AC K1XSI3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Thiol-specific monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MBM_06127 {ECO:0000313|EMBL:EKD15499.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15499.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD15499.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15499.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH921441; EKD15499.1; -; Genomic_DNA.
DR RefSeq; XP_007294016.1; XM_007293954.1.
DR AlphaFoldDB; K1XSI3; -.
DR GeneID; 18762062; -.
DR KEGG; mbe:MBM_06127; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_821533_0_0_1; -.
DR InParanoid; K1XSI3; -.
DR OMA; GRYNAYF; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000006753; 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; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT REGION 304..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 38491 MW; 181FB40919903D56 CRC64;
MAPIKSVAVV GAGPAGAITV DALAQEKAFD TIRVFERRGK AEGCCKAWRE PEKYLGERTV
VVGASISGPD ISHAIADLAE VPLNCVVRGK YHPYISDYAF QHPNIRRRPP ITHITSSRET
NQRTVSFEDG THLTDVDHIV FATGADTYTW TLHFLHFLPN LASTICNNRL PNLYQHVFWQ
PDPTLCFVGA VAAGFTSKVF EWQAVLAARF LAGRIAFPPR EEQQAWERER IGRRGDGVPF
SSLYPHFEEY FEEVRSLAGE PTEDGEGRRL PRSEKWWREG FDRAHLKKRI EVWKRENAEA
RDRIRREEGE ERVMYGEEVP RPSGIQNQRA EMQSQSCL
//
