ID Q5AWB2_EMENI Unreviewed; 694 AA.
AC Q5AWB2; C8VCC2;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE SubName: Full=Phenol 2-monooxygenase, putative (AFU_orthologue AFUA_1G13660) {ECO:0000313|EMBL:CBF78415.1};
GN ORFNames=ANIA_07418 {ECO:0000313|EMBL:CBF78415.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF78415.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; BN001304; CBF78415.1; -; Genomic_DNA.
DR RefSeq; XP_680687.1; XM_675595.1.
DR AlphaFoldDB; Q5AWB2; -.
DR EnsemblFungi; CBF78415; CBF78415; ANIA_07418.
DR GeneID; 2869810; -.
DR KEGG; ani:AN7418.2; -.
DR VEuPathDB; FungiDB:AN7418; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR InParanoid; Q5AWB2; -.
DR OMA; DYWKVFV; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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:SF20; 2-MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G13660)-RELATED; 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:UP000000560}.
FT DOMAIN 12..424
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 461..641
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 694 AA; 78492 MW; 0B2124B99C8A2883 CRC64;
MPGTVPTHED HVDVLIVGAG PAGLMLSTWL SRCGIKTRIV DKRGTKVFNG QADGLQCRTL
EIFDSFGFAH RAWRESNHMI EICLWNPDEN GRIRRSDRIP DTIPQISRFQ QVVLHQGRIE
RFFLDSMKEH SNLTVERGVL PVSFEIDEAK AADFDDYPIS VTLRTLSDKE ATPQQRQQHQ
KSADGQRAVV DDGLFRSNLV ADDTDDLIRA ATADSSRDGQ VELVKAKFLV GCDGAHSWVR
RQAGFKLEGD STDYIWGVLD IVPITDFPDI RHRCAIHSAN AGTIMVIPRE NKLVRLYIQL
QATSYNKNGE KADRSWITPD IILQSAQRII HPYKLDYSYC DWWTAYQIGQ RVGDHFSLHD
RVFLAGDAVH THSPKAGQGM NVSMQDTYNL GWKLAHVVKG YCDPAILKTY ESERRGIAQQ
LIAFDHRFSR LFSGRPARDI IDEEGVSMEE FKATFEKGNE FASGIAVNYD ASLLVAKGSK
IAESNDEYKC RVTSKPQLAT KIDVGKRMPS FKVLNQADAR PWHLQELLKS NGRWRVIVFP
GRLTDPRNMQ RFQQLGQKLG DPDSFIRQYT PPGQPIDSMI EVLTVHAGPR TEIELLDLPE
AFHPNHGDMG WDYWKVYVDD DSYHEGHGQA YANYGIDPSN GASVIIRPDQ YVSWVGDMDD
YEEMARFFSA FMKQQVAGKP GAANVRVPFM TTKL
//
