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Database: UniProt
Entry: B2B7H6_PODAN
LinkDB: B2B7H6_PODAN
Original site: B2B7H6_PODAN 
ID   B2B7H6_PODAN            Unreviewed;       479 AA.
AC   B2B7H6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP73754.1};
DE   SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:CDP26155.1};
GN   ORFNames=PODANS_2_11140 {ECO:0000313|EMBL:CAP73754.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73754.1};
RN   [1] {ECO:0000313|EMBL:CAP73754.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP73754.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP73754.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP73754.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP26155.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; CU640366; CAP73754.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP26155.1; -; Genomic_DNA.
DR   RefSeq; XP_001911926.1; XM_001911891.1.
DR   AlphaFoldDB; B2B7H6; -.
DR   GeneID; 6195956; -.
DR   KEGG; pan:PODANSg8971; -.
DR   VEuPathDB; FungiDB:PODANS_2_11140; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_5_0_1; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
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; IPR000960; Flavin_mOase.
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; 2.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00370; FMOXYGENASE.
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:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:CDP26155.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   REGION          65..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  53987 MW;  39CBF751E7AD81C6 CRC64;
     MGFETVLGQA PFGIHRIAII GAGPCGLAAA KYLVAQKAFE KIDIYEQQSE VGGVWKYSAK
     PAENRRVPQV NPECPPDPPL EPGDGNDDKG PVFPSPMYKL LHTNIPRGLM PFTDFPFSDD
     LLIFPSRDDV QDYLVQYSQD IRHLISFSTE VKDVRLRTDA KGKDQWDVDV LSLRTGELTT
     ATYDAVVVAS GHYSIIYIPD MKGISEFNST HPDIISHSKY YRTPEPFRNK KVIVVGNAAS
     GLDIASQISQ VSQQPLLLSV RTPTPEANLE WTGAEEVPEI EEFLVADRAV RFKEGRVEKD
     IDAIVFATGY LYSFPFLTSL QPPLVTDGRR VRGLYKHLFH IEHPTLVFPG LPIKVVPFPV
     SQSQAATFSR VWANLLPLPS VDDMKRWEDE EAEKKGSKYH VWPVGADSEY INSVYDWITE
     AGIPGKEPPR WDEEQCWQRT IHMKAKLRFE LEGRKAKTLK ELGFDYEPEQ KDDSGPLLL
//
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