ID Q4WS84_ASPFU Unreviewed; 656 AA.
AC Q4WS84;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Phenol 2-monooxygenase, putative {ECO:0000313|EMBL:EAL90698.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:EAL90698.1};
GN ORFNames=AFUA_1G13660 {ECO:0000313|EMBL:EAL90698.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90698.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL90698.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL90698.1}.
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DR EMBL; AAHF01000004; EAL90698.1; -; Genomic_DNA.
DR RefSeq; XP_752736.1; XM_747643.1.
DR AlphaFoldDB; Q4WS84; -.
DR STRING; 330879.Q4WS84; -.
DR EnsemblFungi; EAL90698; EAL90698; AFUA_1G13660.
DR GeneID; 3509832; -.
DR KEGG; afm:AFUA_1G13660; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR InParanoid; Q4WS84; -.
DR OMA; AYWMARC; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
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; 2.
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 ECO:0000313|EMBL:EAL90698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT DOMAIN 9..146
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 202..406
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 446..612
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 656 AA; 74040 MW; 41EBEBF4D8D3C419 CRC64;
MTESSISYTD VLIIGAGPSG LMAAYWMARC GVNARIIDKR GTKVFTGQAD GLRPRTLELL
DSIGVVHRVL HEACEAAEFT FWAPSEDGRL KRQEQHPIHD VNNSPFGNCL LNQGRIERFI
LDAIRDCSDL EVERGVIAES LEYDEALENS SDAYPITVTL RTLSEEDANP SPAHGGSGGV
RNGLFRSNIT PDDWDDLIRK SKERPGNVET VKAKYLIGCD GAHSWTRKQL NIPFEGSTTE
HIWGVVDMVP ITNFPDIRRV CTVETEHGTL LIIPRERQLV RLYLPLQVVD GISGSLDRSS
VTLDMVRQRA KEMLRPFDFD FKVCDWWTVY QVGRRLASNF TKGRIHLAGD AIHTHSPKAG
LGMNMSMQDG FNIGWKMALV AKGVARPSIL ATYELERKRT AQMLIDLDRR LQPLFVKQQQ
SDATESTAPS NGKETLIDVI QLSIAFANGY ACHYGPSSLV HKGGENIAAN LIPGERFPPV
KVRNQADGQA WWTTRLFKSD GRFRIVLLAG DLRHKYQRQR VEAFSAHLAS AESVLQRYRL
EGEKLDSLIE VITIHSAPMR EMDFPDFPEM LRLFDQERGW AYDKIWSDDD CFWDRQCTGK
GYETWGVDRI RGALVILRPD QHIGWVGNIE DVDEMTCYFE QIFQPPQKSV NMEGNA
//
