ID B2B409_PODAN Unreviewed; 635 AA.
AC B2B409;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:CDP31236.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 6, supercontig 2 {ECO:0000313|EMBL:CAP71845.1};
GN ORFNames=PODANS_6_7840 {ECO:0000313|EMBL:CAP71845.1};
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:CAP71845.1};
RN [1] {ECO:0000313|EMBL:CAP71845.1, 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:CAP71845.1};
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:CAP71845.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP71845.1};
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:CDP31236.1}
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 (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; CU638744; CAP71845.1; -; Genomic_DNA.
DR EMBL; FO904941; CDP31236.1; -; Genomic_DNA.
DR RefSeq; XP_001910709.1; XM_001910674.1.
DR AlphaFoldDB; B2B409; -.
DR GeneID; 6194751; -.
DR KEGG; pan:PODANSg7748; -.
DR VEuPathDB; FungiDB:PODANS_6_7840; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000001197; Chromosome 6.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF16; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 9..407
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 433..603
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 635 AA; 70219 MW; 8A7039DEEA19C1CB CRC64;
MSPPASTKVD LFIVGAGPAG LALANWFRGA NIKVLIVDKK PGPTPRGQAE GLKSTTNEIF
DSYGIGPQVT AESWRLEEIA CWGTRKDGGE GIVREQVIPD KVAELGKPRE TMLQQSRVEH
HMLHNILSHD NIEIRYSTAP ISVDVDTSCV HEADTFPVSV SLEKVTTNIN TTNGDTTNGT
NCHATNGHHI NGQNGHQPNE HDAPSDKISA KYIVGCDGAR SWLRKQLDVS LEGDLTDSVF
GVVDIIPKSN FPDIRRVCYL RAASGTILLV PRSNKEVRMY IPVESGTALP DPKDLTFDRV
MDAARKIIAP YTMEVGSVSW WSAYRVRQRV GNHFSRLNER AFLVGDAVHT HSPKAGQGMN
TSIQDAYNLG WKLRLTLEGK VRSSGARQDL LRTYESERRP VALDLIAFDK GFLKLFAAPS
AQFDTEILQA LKFTTGLSIR YPPSCAVQLP KGIEQLGPSL LKADLVPGKR LPDFRVVYQA
DGVPTWMHQR LSATGQFRVI IFAGDISDST ASKRLHDVGK YLGESKSLKH VVMPQSEQEP
LVEVVVVHCA ERDLVDLSAL PEVYRPWSDE SGYDFWRVFA DVESVHDGHG RAYERLEIDR
QVGCTVVVRP DGYIGAVLEV DDVEGVERYF EGMNV
//
